Molecules for disease detection and treatment

ABSTRACT

The present invention provides purified disease detection and treatment molecule polynucleotides (mddt). Also encompassed are the polypeptides (MDDT) encoded by mddt. The invention also provides for the use of mddt, or complements, oligonucleotides, or fragments thereof in diagnostic assays. The invention further provides for vectors and host cells containing mddt for the expression of MDDT. The invention additionally provides for the use of isolated and purified MDDT to induce antibodies and to screen libraries of compounds and the use of anti-MDDT antibodies in diagnostic assays. Also provided are microarrays containing mddt and methods of use.

TECHNICAL FIELD

[0001] The present invention relates to molecules for disease detection and treatment and to the use of these sequences in the diagnosis, study, prevention, and treatment of diseases associated with, as well as effects of exogenous compounds on, the expression of molecules for disease detection and treatment.

BACKGROUND OF THE INVENTION

[0002] The human genome is comprised of thousands of genes, many encoding gene products that function in the maintenance and growth of the various cells and tissues in the body. Aberrant expression or mutations in these genes and their products is the cause of, or is associated with, a variety of human diseases such as cancer and other cell proliferative disorders. The identification of these genes and their products is the basis of an ever-expanding effort to find markers for early detection of diseases, and targets for their prevention and treatment.

[0003] For example, cancer represents a type of cell proliferative disorder that affects nearly every tissue in the body. A wide variety of molecules, either aberrantly expressed or mutated, can be the cause of, or involved with, various cancers because tissue growth involves complex and ordered patterns of cell proliferation, cell differentiation, and apoptosis. Cell proliferation must be regulated to maintain both the number of cells and their spatial organization. This regulation depends upon the appropriate expression of proteins which control cell cycle progression in response to extracellular signals such as growth factors and other mitogens, and intracellular cues such as DNA damage or nutrient starvation. Molecules which directly or indirectly modulate cell cycle progression fall into several categories, including growth factors and their receptors, second messenger and signal transduction proteins, oncogene products, tumor-suppressor proteins, and mitosis-promoting factors. Aberrant expression or mutations in any of these gene products can result in cell proliferative disorders such as cancer. Oncogenes are genes generally derived from normal genes that, through abnormal expression or mutation, can effect the transformation of a normal cell to a malignant one (oncogenesis). Oncoproteins, encoded by oncogenes, can affect cell proliferation in a variety of ways and include growth factors, growth factor receptors, intracellular signal transducers, nuclear transcription factors, and cell-cycle control proteins. In contrast, tumor-suppressor genes are involved in inhibiting cell proliferation. Mutations which cause reduced or loss of function in tumor-suppressor genes result in aberrant cell proliferation and cancer. Thus a wide variety of genes and their products have been found that are associated with cell proliferative disorders such as cancer, but many more may exist that are yet to be discovered.

[0004] DNA-based arrays can provide a simple way to explore the expression of a single polymorphic gene or a large number of genes. When the expression of a single gene is explored, DNA-based arrays are employed to detect the expression of specific gene variants. For example, a p53 tumor suppressor gene array is used to determine whether individuals are carrying mutations that predispose them to cancer. A cytochrome p450 gene array is useful to determine whether individuals have one of a number of specific mutations that could result in increased drug metabolism, drug resistance or drug toxicity.

[0005] DNA-based array technology is especially relevant for the rapid screening of expression of a large number of genes. There is a growing awareness that gene expression is affected in a global fashion. A genetic predisposition, disease or therapeutic treatment may affect, directly or indirectly, the expression of a large number of genes. In some cases the interactions may be expected, such as when the genes are part of the same signaling pathway. In other cases, such as when the genes participate in separate signaling pathways, the interactions may be totally unexpected. Therefore, DNA-based arrays can be used to investigate how genetic predisposition, disease, or therapeutic treatment affects the expression of a large number of genes.

[0006] The discovery of new molecules for disease detection and treatment satisfies a need in the art by providing new compositions which are useful in the diagnosis, study, prevention, and treatment of diseases associated with, as well as effects of exogenous compounds on, the expression of molecules for disease detection and treatment.

SUMMARY OF THE INVENTION

[0007] The present invention relates to human disease detection and treatment molecule polynucleotides (mddt) as presented in the Sequence Listing. The mddt uniquely identify genes encoding structural, functional, and regulatory disease detection and treatment molecules.

[0008] The invention provides an isolated polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). In one alternative, the polynucleotide comprises a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252. In another alternative, the polynucleotide comprises at least 30 contiguous nucleotides of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide comprising a polynucleotide sequence at lease identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). In another alternative, the polynucleotide comprises at least 60 contiguous nucleotides of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide comprising a polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). The invention further provides a composition for the detection of expression of disease detection and treatment molecule polynucleotides comprising at least one isolated polynucleotide comprising a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d); and a detectable label.

[0009] The invention also provides a method for detecting a target polynucleotide in a sample, said target polynucleotide having a polynucleotide sequence of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence of a polynucleotide selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). The method comprises a) amplifying said target polynucleotide or fragment thereof using polymerase chain reaction amplification, and b) detecting the presence or absence of said amplified target polynucleotide or fragment thereof, and, optionally, if present, the amount thereof.

[0010] The invention also provides a method for detecting a target polynucleotide in a sample, said target polynucleotide having a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). The method comprises a) hybridizing the sample with a probe comprising at least 60 contiguous nucleotides comprising a sequence complementary to said target polynucleotide in sample, and which probe specifically hybridizes to said target polynucleotide, under conditions whereby a hybridization complex is formed between said probe and said target polynucleotide, and b) detecting the presence or absence of said hybridization complex, and, optionally, if present, the amount thereof. In one alternative, the invention provides a composition comprising a target polynucleotide of the method, wherein said probe comprises at least 30 contiguous nucleotides. In one alternative, the invention provides a composition comprising a target polynucleotide of the method, wherein said probe comprises at least 60 contiguous nucleotides.

[0011] The invention further provides a recombinant polynucleotide comprising a promoter sequence operably linked to an isolated polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). In one alternative, the invention provides a cell transformed with the recombinant polynucleotide. In another alternative, the invention provides a transgenic organism comprising the recombinant polynucleotide.

[0012] The invention also provides a method for producing a disease detection and treatment polypeptide, the method comprising a) culturing a cell under conditions suitable for expression of the disease detection and treatment polypeptide, wherein said cell is transformed with a recombinant polynucleotide, said recombinant polynucleotide comprising an isolated polynucleotide selected from the group consisting of i) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; ii) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; iii) a polynucleotide complementary to the polynucleotide of i); iv) a polynucleotide complementary to the polynucleotide of ii); and v) an RNA equivalent of i) through iv), and b) recovering the disease detection and treatment polypeptide so expressed. The invention additionally provides a method wherein the polypeptide has an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.

[0013] The invention also provides an isolated disease detection and treatment polypeptide (MDDT) encoded by at least one polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252. The invention further provides a method of screening for a test compound that specifically binds to the polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. The method comprises a) combining the polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506 with at least one test compound under suitable conditions, and b) detecting binding of the polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506 to the test compound, thereby identifying a compound that specifically binds to the polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.

[0014] The invention further provides a microarray wherein at least one element of the microarray is an isolated polynucleotide comprising at least 30 contiguous nucleotides of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). The invention also provides a method for generating a transcript image of a sample which contains polynucleotides. The method comprises a) labeling the polynucleotides of the sample, b) contacting the elements of the microarray with the labeled polynucleotides of the sample under conditions suitable for the formation of a hybridization complex, and c) quantifying the expression of the polynucleotides in the sample.

[0015] Additionally, the invention provides a method for screening a compound for effectiveness in altering expression of a target polynucleotide, wherein said target polynucleotide comprises a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; c) a polynucleotide complementary to the polynucleotide of a); d) a polynucleotide complementary to the polynucleotide of b); and e) an RNA equivalent of a) through d). The method comprises a) exposing a sample comprising the target polynucleotide to a compound, b) detecting altered expression of the target polynucleotide, and c) comparing the expression of the target polynucleotide in the presence of varying amounts of the compound and in the absence of the compound.

[0016] The invention further provides a method for assessing toxicity of a test compound, said method comprising a) treating a biological sample containing nucleic acids with the test compound; b) hybridizing the nucleic acids of the treated biological sample with a probe comprising at least 20 contiguous nucleotides of a polynucleotide selected from the group consisting of i) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; ii) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252; iii) a polynucleotide complementary to the polynucleotide of i); iv) a polynucleotide complementary to the polynucleotide of ii); and v) an RNA equivalent of i) through iv). Hybridization occurs under conditions whereby a specific hybridization complex is formed between said probe and a target polynucleotide in the biological sample, said target polynucleotide comprising a polynucleotide sequence of a polynucleotide selected from the group consisting of i) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:11-252; ii) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:11-252; iii) a polynucleotide complementary to the polynucleotide of i); iv) a polynucleotide complementary to the polynucleotide of ii); and v) an RNA equivalent of i) through iv), and alternatively, the target polynucleotide comprises a polynucleotide sequence of a fragment of a polynucleotide selected from the group consisting of i-v above; c) quantifying the amount of hybridization complex; and d) comparing the amount of hybridization complex in the treated biological sample with the amount of hybridization complex in an untreated biological sample, wherein a difference in the amount of hybridization complex in the treated biological sample is indicative of toxicity of the test compound.

[0017] The invention further provides an isolated polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. In one alternative, the invention provides an isolated polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.

[0018] The invention further provides an isolated polynucleotide encoding a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. In one alternative, the polynucleotide encodes a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. In another alternative, the polynucleotide comprises a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252.

[0019] Additionally, the invention provides an isolated antibody which specifically binds to a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.

[0020] The invention further provides a composition comprising a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and a pharmaceutically acceptable excipient. In one embodiment, the composition comprises a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. The invention additionally provides a method of treating a disease or condition associated with decreased expression of functional MDDT, comprising administering to a patient in need of such treatment the composition.

[0021] The invention also provides a method for screening a compound for effectiveness as an agonist of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. The method comprises a) exposing a sample comprising the polypeptide to a compound, and b) detecting agonist activity in the sample. In one alternative, the invention provides a composition comprising an agonist compound identified by the method and a pharmaceutically acceptable excipient. In another alternative, the invention provides a method of treating a disease or condition associated with decreased expression of functional MDDT, comprising administering to a patient in need of such treatment the composition.

[0022] Additionally, the invention provides a method for screening a compound for effectiveness as an antagonist of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. The method comprises a) exposing a sample comprising the polypeptide to a compound, and b) detecting antagonist activity in the sample. In one alternative, the invention provides a composition comprising an antagonist compound identified by the method and a pharmaceutically acceptable excipient. In another alternative, the invention provides a method of treating a disease or condition associated with overexpression of functional MDDT, comprising administering to a patient in need of such treatment the composition.

[0023] The invention further provides a method of screening for a compound that modulates the activity of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506. The method comprises a) combining the polypeptide with at least one test compound under conditions permissive for the activity of the polypeptide. b) assessing the activity of the polypeptide in the presence of the test compound, and c) comparing the activity of the polypeptide in the presence of the test compound with the activity of the polypeptide in the absence of the test compound, wherein a change in the activity of the polypeptide in the presence of the test compound is indicative of a compound that modulates the activity of the polypeptide.

DESCRIPTION OF THE TABLES

[0024] Table 1 shows the sequence identification numbers (SEQ ID NO:s) and template identification numbers (template IDs) corresponding to the polynucleotides of the present invention, along with the sequence identification numbers (SEQ ID NO:s) and open reading frame identification numbers (ORF IDs) corresponding to polypeptides encoded by the template ID.

[0025] Table 2 shows the sequence identification numbers (SEQ ID NO:s) and template identification numbers (template IDs) corresponding to the polynucleotides of the present invention, along with their GenBank hits (GI Numbers), probability scores, and functional annotations corresponding to the GenBank hits.

[0026] Table 3 shows the sequence identification numbers (SEQ ID NO:s) and template identification numbers (template IDs) corresponding to the polynucleotides of the present invention, along with polynucleotide segments of each template sequence as defined by the indicated “start” and “stop” nucleotide positions. The reading frames of the polynucleotide segments and the Pfam hits. Pfam descriptions, and E-values corresponding to the polypeptide domains encoded by the polynucleotide segments are indicated.

[0027] Table 4 shows the sequence identification numbers (SEQ ID NO:s) and template identification numbers (template IDs) corresponding to the polynucleotides of the present invention, along with polynucleotide segments of each template sequence as defined by the indicated “start” and “stop” nucleotide positions. The reading frames of the polynucleotide segments are shown, and the polypeptides encoded by the polynucleotide segments constitute either signal peptide (SP) or transmembrane (TM) domains, as indicated. The membrane topology of the encoded polypeptide sequence is indicated, the N-terminus (N) listed as being oriented to either the cytosolic (N in) or non-cytosolic (N out) side of the cell membrane or organelle.

[0028] Table 5 shows the sequence identification numbers (SEQ ID NO:s) and template identification numbers (template IDs) corresponding to the polynucleotides of the present invention, along with component sequence identification numbers (component IDs) corresponding to each template. The component sequences, which were used to assemble the template sequences, are defined by the indicated “start” and “stop” nucleotide positions along each template.

[0029] Table 6 shows the tissue distribution profiles for the templates of the invention.

[0030] Table 7 shows the sequence identification numbers (SEQ ID NO:s) corresponding to the polypeptides of the present invention, along with the reading frames used to obtain the polypeptide segments, the lengths of the polypeptide segments, the “start” and “stop” nucleotide positions of the polynucleotide sequences used to define the encoded polypeptide segments, the GenBank hits (GI Numbers), probability scores, and functional annotations corresponding to the GenBank hits.

[0031] Table 8 summarizes the bioinformatics tools which are useful for analysis of the polynucleotides of the present invention. The first column of Table 8 lists analytical tools, programs, and algorithms, the second column provides brief descriptions thereof, the third column presents appropriate references, all of which are incorporated by reference herein in their entirety, and the fourth column presents, where applicable, the scores, probability values, and other parameters used to evaluate the strength of a match between two sequences (the higher the score, the greater the homology between two sequences).

DETAILED DESCRIPTION OF THE INVENTION

[0032] Before the nucleic acid sequences and methods are presented, it is to be understood that this invention is not limited to the particular machines, methods, and materials described. Although particular embodiments are described, machines, methods, and materials similar or equivalent to these embodiments may be used to practice the invention. The preferred makes, methods, and materials set forth are not intended to limit the scope of the invention which is limited only by the appended claims.

[0033] The singular forms “a”, “an”, and “the” include plural reference unless the context clearly dictates otherwise. All technical and scientific terms have the meanings commonly understood by one of ordinary skill in the art. All publications are incorporated by reference for the purpose of describing and disclosing the cell lines, vectors, and methodologies which are presented and which might be used in connection with the invention. Nothing in the specification is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention.

[0034] Definitions

[0035] As used herein, the lower case “mddt” refers to a nucleic acid sequence, while the upper case “MDDT” refers to an amino acid sequence encoded by mddt. A “full-length” mddt refers to a nucleic acid sequence containing the entire coding region of a gene endogenously expressed in human tissue.

[0036] “Adjuvants” are materials such as Freund's adjuvant, mineral gels (aluminum hydroxide), and surface active substances (lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, keyhole limpet hemocyanin, and dinitrophenol) which may be administered to increase a host's immunological response.

[0037] “Allele” refers to an alternative form of a nucleic acid sequence. Alleles result from a “mutation,” a change or an alternative reading of the genetic code. Any given gene may have none, one, or many allelic forms. Mutations which give rise to alleles include deletions, additions, or substitutions of nucleotides. Each of these changes may occur alone, or in combination with the others, one or more times in a given nucleic acid sequence. The present invention encompasses allelic mddt.

[0038] “Amino acid sequence” refers to a peptide, a polypeptide, or a protein of either natural or synthetic origin. The amino acid sequence is not limited to the complete, endogenous amino acid sequence and may be a fragment, epitope, variant, or derivative of a protein expressed by a nucleic acid sequence.

[0039] “Amplification” refers to the production of additional copies of a sequence and is carried out using polymerase chain reaction (PCR) technologies well known in the art.

[0040] “Antibody” refers to intact molecules as well as to fragments thereof, such as Fab, F(ab′)₂, and Fv fragments, which are capable of binding the epitopic determinant. Antibodies that bind MDDT polypeptides can be prepared using intact polypeptides or using fragments containing small peptides of interest as the immunizing antigen. The polypeptide or peptide used to immunize an animal (e.g., a mouse, a rat, or a rabbit) can be derived from the translation of RNA, or synthesized chemically, and can be conjugated to a carrier protein if desired. Commonly used carrier that are chemically coupled to peptides include bovine serum albumin, thyroglobulin, and keyhole limpet hemocyanin (KLH). The coupled peptide is then used to immunize the animal.

[0041] “Antisense sequence” refers to a sequence capable of specifically hybridizing to a target sequence. The antisense sequence may include DNA, RNA, or any nucleic acid mimic or analog such as peptide nucleic acid (PNA); oligonucleotides having modified backbone linkages such as phosphorothioates, methylphosphonates, or benzylphosphonates; oligonucleotides having modified sugar groups such as 2′-methoxyethyl sugars or 2′-methoxyethoxy sugars; or oligonucleotides having modified bases such as 5-methyl cytosine, 2′-deoxyuracil, or 7-deaza-2′-deoxyguanosine.

[0042] “Antisense sequence” refers to a sequence capable of specifically hybridizing to a target sequence. The antisense sequence can be DNA, RNA, or any nucleic acid mimic or analog.

[0043] “Antisense technology” refers to any technology which relies on the specific hybridization of an antisense sequence to a target sequence.

[0044] A “bin” is a portion of computer memory space used by a computer program for storage of data, and bounded in such a manner that data stored in a bin may be retrieved by the program.

[0045] “Biologically active” refers to an amino acid sequence having a structural, regulatory, or biochemical function of a naturally occurring amino acid sequence.

[0046] “Clone joining” is a process for combining gene bins based upon the bins' containing sequence information from the same clone. The sequences may assemble into a primary gene transcript as well as one or more splice variants.

[0047] “Complementary” describes the relationship between two single-stranded nucleic acid sequences that anneal by base-pairing (5′-A-G-T-3′ pairs with its complement 3′-T-C-A-5′).

[0048] A “component sequence” is a nucleic acid sequence selected by a computer program such as PHRED and used to assemble a consensus or template sequence from one or more component sequences.

[0049] A “consensus sequence” or “template sequence” is a nucleic acid sequence which has been assembled from overlapping sequences, using a computer program for fragment assembly such as the GELVIEW fragment assembly system (Genetics Computer Group (GCG), Madison Wis.) or using a relational database management system (RDMS).

[0050] “Conservative amino acid substitutions” are those substitutions that, when made, least interfere with the properties of the original protein, i.e., the structure and especially the function of the protein is conserved and not significantly changed by such substitutions. The table below shows amino acids which may be substituted for an original amino acid in a protein and which are regarded as conservative substitutions. Original Residue Conservative Substitution Ala Gly, Ser Arg His, Lys Asn Asp, Gln, His Asp Asn, Glu Cys Ala, Ser Gln Asn, Glu, His Glu Asp, Gln, His Gly Ala His Asn, Arg, Gln, Glu Ile Leu, Val Leu Ile, Val Lys Arg, Gln, Glu Met Leu, Ile Phe His, Met, Leu, Trp, Tyr Ser Cys, Thr Thr Ser, Val Trp Phe, Tyr Tyr His, Phe, Trp Val Ile, Leu, Thr

[0051] Conservative substitutions generally maintain (a) the structure of the polypeptide backbone in the area of the substitution, for example, as a beta sheet or alpha helical conformation, (b) the charge or hydrophobicity of the molecule at the target site, or (c) the bulk of the side chain.

[0052] “Deletion” refers to a change in either a nucleic or amino acid sequence in which at least one nucleotide or amino acid residue, respectively, is absent.

[0053] “Derivative” refers to the chemical modification of a nucleic acid sequence, such as by replacement of hydrogen by an alkyl, acyl, amino, hydroxyl, or other group.

[0054] “Differential expression” refers to increased or upregulated; or decreased, downregulated, or absent gene or protein expression, determined by comparing at least two different samples. Such comparisons may be carried out between, for example, a treated and an untreated sample, or a diseased and a normal sample.

[0055] The terms “element” and “array element” refer to a polynucleotide, polypeptide, or other chemical compound having a unique and defined position on a microarray.

[0056] “E-value” refers to the statistical probability that a match between two sequences occurred by chance.

[0057] “Exon shuffling” refers to the recombination of different coding regions (exons). Since an exon may represent a structural or functional domain of the encoded protein, new proteins may be assembled through the novel reassortment of stable substructures, thus allowing acceleration of the evolution of new protein functions.

[0058] A “fragment” is a unique portion of mddt or MDDT which is identical in sequence to but shorter in length than the parent sequence. A fragment may comprise up 0 the entire length of the defined sequence, minus one nucleotide/amino acid residue. For example, a fragment may comprise from 10 to 1000 contiguous amino acid residues or nucleotides. A fragment used as a probe, primer, antigen, therapeutic molecule, or for other purposes, may be at least 5, 10, 15, 16, 20, 25, 30, 40, 50, 60, 75, 100, 150, 250 or at least 500 contiguous amino acid residues or nucleotides in length. Fragments may be preferentially selected from certain regions of a molecule. For example, a polypeptide fragment may comprise a certain length of contiguous amino acids selected from the first 250 or 500 amino acids (or first 25% or 50%) of a polypeptide as shown in a certain defined sequence. Clearly these lengths are exemplary, and any length that is supported by the specification, including the Sequence Listing and the figures, may be encompassed by the present embodiments.

[0059] A fragment of mddt comprises a region of unique polynucleotide sequence that specifically identifies mddt, for example, as distinct from any other sequence in the same genome. A fragment of mddt is useful, for example, in hybridization and amplification technologies and in analogous methods that distinguish mddt from related polynucleotide sequences. The precise length of a fragment of mddt and the region of mddt to which the fragment corresponds are routinely determinable by one of ordinary skill in the art based on the intended purpose for the fragment.

[0060] A fragment of MDDT is encoded by a fragment of mddt. A fragment of MDDT comprises a region of unique amino acid sequence that specifically identifies MDDT. For example, a fragment of MDDT is useful as an immunogenic peptide for the development of antibodies that specifically recognize MDDT. The precise length of a fragment of MDDT and the region of MDDT to which the fragment corresponds are routinely determinable by one of ordinary skill in the art based on the intended purpose for the fragment.

[0061] A “full length” nucleotide sequence is one containing at least a start site for translation to a protein sequence, followed by an open reading frame and a stop site, and encoding a “full length” polypeptide.

[0062] “Hit” refers to a sequence whose annotation will be used to describe a given template. Criteria for selecting the top hit are as follows: if the template has one or more exact nucleic acid matches, the top hit is the exact match with highest percent identity. If the template has no exact matches but has significant protein hits, the top hit is the protein hit with the lowest E-value. If the template has no significant protein hits, but does have significant non-exact nucleotide hits, the top hit is the nucleotide hit with the lowest E-value.

[0063] “Homology” refers to sequence similarity either between a reference nucleic acid sequence and at least a fragment of an mddt or between a reference amino acid sequence and a fragment of an MDDT.

[0064] “Hybridization”refers to the process by which a strand of nucleotides anneals with a complementary strand through base pairing. Specific hybridization is an indication that two nucleic acid sequences share a high degree of identity. Specific hybridization complexes form under defined annealing conditions, and remain hybridized after the “washing” step. The defined hybridization conditions include the annealing conditions and the washing step(s), the latter of which is particularly important in determining the stringency of the hybridization process, with more stringent conditions allowing less non-specific binding, i.e., binding between pairs of nucleic acid probes that are not perfectly matched. Permissive conditions for annealing of nucleic acid sequences are routinely determinable and may be consistent among hybridization experiments, whereas wash conditions may be varied among experiments to achieve the desired stringency.

[0065] Generally, stringency of hybridization is expressed with reference to the temperature under which the wash step is carried out. Generally, such wash temperatures are selected to be about 5° C. to 20° C. lower than the thermal melting point (T_(m)) for the specific sequence at a defined ionic strength and pH. The T_(m) is the temperature (under defined ionic strength and pH) at which 50% of the target sequence hybridizes to a perfectly matched probe. An equation for calculating T_(m) and conditions for nucleic acid hybridization is well known and can be found in Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, 2^(nd) ed., vol. 1-3, Cold Spring Harbor Press, Plainview N.Y.; specifically see volume 2, chapter 9.

[0066] High stringency conditions for hybridization between polynucleotides of the present invention include wash conditions of 68° C. in the presence of about 0.2×SSC and about 0.1% SDS, for 1 hour. Alternatively, temperatures of about 65° C., 60° C., or 55° C. may be used. SSC concentration may be varied from about 0.2 to 2×SSC, with SDS being present at about 0.1%. Typically, blocking reagents are used to block non-specific hybridization. Such blocking reagents include, for instance, denatured salmon sperm DNA at about 100-200 μg/ml. Useful variations on these conditions will be readily apparent to those skilled in the art. Hybridization, particularly under high stringency conditions, may be suggestive of evolutionary similarity between the nucleotides. Such similarity is strongly indicative of a similar role for the nucleotides and their resultant proteins.

[0067] Other parameters, such as temperature, salt concentration, and detergent concentration may be varied to achieve the desired stringency. Denaturants, such as formamide at a concentration of about 35-50% v/v, may also be used under particular circumstances, such as RNA:DNA hybridizations. Appropriate hybridization conditions are routinely determinable by one of ordinary skill in the art.

[0068] “Immunologically active” or “immunogenic” describes the potential for a natural, recombinant, or synthetic peptide, epitope, polypeptide, or protein to induce antibody production in appropriate animals, cells, or cell lines.

[0069] “Insertion” or “assertion” refers to a change in either a nucleic or an amino acid sequence in which at least one nucleon or residue, respectively, is added to the sequence.

[0070] “Labeling” refers to the covalent or noncovalent joining of a polynucleotide, polypeptide, or antibody with a reporter molecule capable of producing a detectable or measurable signal.

[0071] “Microarray” is any arrangement of nucleic acids, amino acids, antibodies, etc., on a substrate. The substrate may be a solid support such as beads, glass, paper, nitrocellulose, nylon, or an appropriate membrane.

[0072] “Linkers” are short stretches of nucleotide sequence which may be added to a vector or an mddt to create restriction endonuclease sites to facilitate cloning. “Polylinkers” are engineered to incorporate multiple restriction enzyme sites and to provide for the use of enzymes which leave 5′ or 3′ overhangs (e.g., BamHI, EcoRI, and HindIII) and those which provide blunt ends (e.g., EcoRV, SnaBI, and StuI).

[0073] “Naturally occurring” refers to an endogenous polynucleotide or polypeptide that may be isolated from viruses or prokaryotic or eukaryotic cells.

[0074] “Nucleic acid sequence” refers to the specific order of nucleotides joined by phosphodiester bonds in a linear, polymeric arrangement. Depending on the number of nucleotides, the nucleic acid sequence can be considered an oligomer, oligonucleotide, or polynucleotide. The nucleic acid can be DNA, RNA, or any nucleic acid analog, such as PNA, may be of genomic or synthetic origin, may be either double-stranded or single-stranded, and can represent either the sense or antisense (complementary) strand.

[0075] “Oligomer” refers to a nucleic acid sequence of at least about 6 nucleotides and as many as about 60 nucleotides, preferably about 15 to 40 nucleotides, and most preferably between about 20 and 30 nucleotides, that may be used in hybridization or amplification technologies. Oligomers may be used as, e.g., primers for PCR, and are usually chemically synthesized.

[0076] “Operably linked” refers to the situation in which a first nucleic acid sequence is placed in a functional relationship with the second nucleic acid sequence. For instance, a promoter is operably linked to a coding sequence if the promoter affects the transcription or expression of the coding sequence. Generally, operably linked DNA sequences may be in close proximity or contiguous and, where necessary to join two protein coding regions, in the same reading frame.

[0077] “Peptide nucleic acid” (PNA) refers to a DNA mimic in which nucleotide bases are attached to a pseudopeptide backbone to increase stability. PNAs, also designated antigene agents, can prevent gene expression by targeting complementary messenger RNA.

[0078] The phrases “percent identity” and “% identity”, as applied to polynucleotide sequences, refer to the percentage of residue matches between at least two polynucleotide sequences aligned using a standardized algorithm. Such an algorithm may insert, in a standardized and reproducible way, gaps in the sequences being compared in order to optimize alignment between two sequences, and therefore achieve a more meaningful comparison of the two sequences.

[0079] Percent identity between polynucleotide sequences may be determined using the default parameters of the CLUSTAL V algorithm as incorporated into the MEGALIGN version 3.12e sequence alignment program. This program is part of the LASERGENE software package, a suite of molecular biological analysis programs (DNASTAR, Madison Wis.). CLUSTAL V is described in Higgins, D. G. and Sharp, P. M. (1989) CABIOS 5:151-153 and in Higgins, D. G. et al. (1992) CABIOS 8:189-191. For pairwise alignments of polynucleotide sequences, the default parameters are set as follows: Ktuple=2, gap penalty=5, window=4, and “diagonals saved”=4. The “weighted” residue weight table is selected as the default. Percent identity is reported by CLUSTAL V as the “percent similarity” between aligned polynucleotide sequence pairs.

[0080] Alternatively, a suite of commonly used and freely available sequence comparison algorithms is provided by the National Center for Biotechnology Information (NCBI) Basic Local Alignment Search Tool (BLAST) (Altschul, S. F. et al. (1990) J. Mol. Biol. 215:403-410), which is available from several sources, including the NCBI, Bethesda, Md., and on the Internet at http://www.ncbi.nlm.nih.gov/BLAST/. The BLAST software suite includes various sequence analysis programs including “blastn,” that is used to determine alignment between a known polynucleotide sequence and other sequences on a variety of databases. Also available is a tool called “BLAST 2 Sequences” that is used for direct pairwise comparison of two nucleotide sequences. “BLAST 2 Sequences” can be accessed and used interactively at http://www.ncbi.nim.nih.gov/gorf/bl2/. The “BLAST 2 Sequences” tool can be used for both blastn and blastp (discussed below). BLAST programs are commonly used with gap and other parameters set to default settings. For example, to compare two nucleotide sequences, one may use blastn with the “BLAST 2 Sequences” tool Version 2.0.9 (May-07-1999) set at default parameters. Such default parameters may be, for example:

[0081] Matrix: BLOSUM62

[0082] Reward for match: 1

[0083] Penalty for mismatch: −2

[0084] Open Gap: 5 and Extension Gap: 2 penalties

[0085] Gap x drop-off: 50

[0086] Expect: 10

[0087] Word Size: 11

[0088] Filter: on

[0089] Percent identity may be measured over the length of an entire defined sequence, for example, as defined by a particular SEQ ID number, or may be measured over a shorter length, for example, over the length of a fragment taken from a larger, defined sequence, for instance, a fragment of at least 20, at least 30, at least 40, at least 50, at least 70, at least 100, or at least 200 contiguous nucleotides. Such lengths are exemplary only, and it is understood that any fragment length supported by the sequences shown herein, in figures or Sequence Listings, may be used to describe a length over which percentage identity may be measured.

[0090] Nucleic acid sequences that do not show a high degree of identity may nevertheless encode similar amino acid sequences due to the degeneracy of the genetic code. It is understood that changes in nucleic acid sequence can be made using this degeneracy to produce multiple nucleic acid sequences that all encode substantially the same protein.

[0091] The phrases “percent identity” and “% identity”, as applied to polypeptide sequences, refer to the percentage of residue matches between at least two polypeptide sequences aligned using a standardized algorithm. Methods of polypeptide sequence alignment are well-known. Some alignment methods take into account conservative amino acid substitutions. Such conservative substitutions, explained in more detail above, generally preserve the hydrophobicity and acidity of the substituted residue, thus preserving the structure (and therefore function) of the folded polypeptide.

[0092] Percent identity between polypeptide sequences may be determined using the default parameters of the CLUSTAL V algorithm as incorporated into the MEGALIGN version 3.12e sequence alignment program (described and referenced above). For pairwise alignments of polypeptide sequences using CLUSTAL V, the default parameters are set as follows: Ktuple=1, gap penalty=3, window=5, and “diagonals saved”=5. The PAM250 matrix is selected as the default residue weight table. As with polynucleotide alignments, the percent identity is reported by CLUSTAL V as the “percent similarity” between aligned polypeptide sequence pairs.

[0093] Alternatively the NCBI BLAST software suite may be used. For example, for a pairwise comparison of two polypeptide sequences, one may use the “BLAST 2 Sequences” tool Version 2.0.9 (May-07-1999) with blastp set at default parameters. Such default parameters may be, for example:

[0094] Matrix: BLOSUM62

[0095] Open Gap: 11 and Extension Gap: 1 penalty

[0096] Gap x drop-off: 50

[0097] Expect: 10

[0098] Word Size: 3

[0099] Filter: on

[0100] Percent identity may be measured over the length of an entire defined polypeptide sequence, for example, as defined by a particular SEQ ID number, or may be measured over a shorter length, for example, over the length of a fragment taken from a larger, defined polypeptide sequence, for instance, a fragment of at least 15, at least 20, at least 30, at least 40, at least 50, at least 70 or at least 150 contiguous residues. Such lengths are exemplary only, and it is understood that any fragment length supported by the sequences shown herein, in figures or Sequence listings, may be used to describe a length over which percentage identity may be measured.

[0101] “Post-translational modification” of an MDDT may involve lipidation, glycosylation, phosphorylation, acetylation, racemization, proteolytic cleavage, and other modifications known in the art. These processes may occur synthetically or biochemically. Biochemical modifications will vary by cell type depending on the enzymatic milieu and the MDDT.

[0102] “Probe” refers to mddt or fragments thereof, which are used to detect identical, allelic or related nucleic acid sequences. Probes are isolated oligonucleotides or polynucleotides attached to a detectable label or reporter molecule. Typical labels include radioactive isotopes, ligands, chemiluminescent agents, and enzymes. “Primers” are short nucleic acids, usually DNA oligonucleotides, which may be annealed to a target polynucleotide by complementary base-pairing. The primer may then be extended along the target DNA strand by a DNA polymerase enzyme. Primer pairs can be used for amplification (and identification) of a nucleic acid sequence, e.g., by the polymerase chain reaction (PCR).

[0103] Probes and primers as used in the present invention typically comprise at least 15 contiguous nucleotides of a known sequence. In order to enhance specificity, longer probes and primers may also be employed, such as probes and primers that comprise at least 20, 30, 40, 50, 60, 70, 80, 90, 100, or at least 150 consecutive nucleotides of the disclosed nucleic acid sequences. Probes and primers may be considerably longer than these examples, and it is understood that any length supported by the specification, including the figures and Sequence Listing, may be used.

[0104] Methods for preparing and using probes and primers are described in the references, for example Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, 2^(nd) ed., vol. 1-3, Cold Spring Harbor Press, Plainview N.Y.; Ausubel et al.,1987, Current Protocols in Molecular Biology, Greene Publ. Assoc. & Wiley-Intersciences, New York N.Y.; Innis et al., 1990, PCR Protocols, A Guide to Methods and Applications, Academic Press, San Diego Calif. PCR primer pairs can be derived from a known sequence, for example, by using computer programs intended for that purpose such as Primer (Version 0.5, 1991, Whitehead Institute for Biomedical Research, Cambridge Mass.).

[0105] Oligonucleotides for use as primers are selected using software known in the art for such purpose. For example, OLIGO 4.06 software is useful for the selection of PCR primer pairs of up to 100 nucleotides each, and for the analysis of oligonucleotides and larger polynucleotides of up to 5,000 nucleotides from an input polynucleotide sequence of up to 32 kilobases. Similar primer selection programs have incorporated additional features for expanded capabilities. For example, the PrimOU primer selection program (available to the public from the Genome Center at University of Texas South West Medical Center, Dallas Tex.) is capable of choosing specific primers from megabase sequences and is thus useful for designing primers on a genome-wide scope. The Primer3 primer selection program (available to the public from the Whitehead Institute/

Center for Genome Research, Cambridge Mass.) allows the user to input a “mispriming library.” in which sequences to avoid as primer binding sites are user-specified. Primer3 is useful, in particular, for the selection of oligonucleotides for microarrays. (The source code for the latter two primer selection programs may also be obtained from their respective sources and modified to meet the user's specific needs.) The PrimeGen program (available to the public from the UK Human Genome Mapping Project Resource Centre, Cambridge UK) designs primers based on multiple sequence alignments, thereby allowing selection of primers that hybridize to either the most conserved or least conserved regions of aligned nucleic acid sequences. Hence, this program is useful for identification of both unique and conserved oligonucleotides and polynucleotide fragments. The oligonucleotides and polynucleotide fragments identified by any of the above selection methods are useful in hybridization technologies, for example, as PCR or sequencing primers, microarray elements, or specific probes to identify fully or partially complementary polynucleotides in a sample of nucleic acids. Methods of oligonucleotide selection are not limited to those described above.

[0106] “Purified” refers to molecules, either polynucleotides or polypeptides that are isolated or separated from their natural environment and are at least 60% free, preferably at least 75% free, and most preferably at least 90% free from other compounds with which they are naturally associated.

[0107] A “recombinant nucleic acid” is a sequence that is not naturally occurring or has a sequence that is made by an artificial combination of two or more otherwise separated segments of sequence. This artificial combination is often accomplished by chemical synthesis or, more commonly, by the artificial manipulation of isolated segments of nucleic acids, e.g., by genetic engineering techniques such as those described in Sambrook, supra. The term recombinant includes nucleic acids that have been altered solely by addition, substitution, or deletion of a portion of the nucleic acid. Frequently, a recombinant nucleic acid may include a nucleic acid sequence operably linked to a promoter sequence. Such a recombinant nucleic acid may be part of a vector that is used, for example, to transform a cell.

[0108] Alternatively, such recombinant nucleic acids may be part of a viral vector, e.g., based on a vaccinia virus, that could be use to vaccinate a mammal wherein the recombinant nucleic acid is expressed, inducing a protective immunological response in the mammal.

[0109] “Regulatory element” refers to a nucleic acid sequence from nontranslated regions of a gene, and includes enhancers, promoters, introns, and 3′ untranslated regions, which interact with host proteins to carry out or regulate transcription or translation.

[0110] “Reporter” molecules are chemical or biochemical moieties used for labeling a nucleic acid, an amino acid, or an antibody. They include radionuclides; enzymes; fluorescent, chemiluminescent, or chromogenic agents; substrates; cofactors; inhibitors; magnetic particles; and other moieties known in the art.

[0111] An “RNA equivalent” in reference to a DNA sequence, is composed of the same linear sequence of nucleotides as the reference DNA sequence with the exception that all occurrences of the nitrogenous base thymine are replaced with uracil, and the sugar backbone is composed of ribose instead of deoxyribose.

[0112] “Sample” is used in its broadest sense. Samples may contain nucleic or amino acids, antibodies, or other materials, and may be derived from any source (e.g., bodily fluids including, but not limited to, saliva, blood, and urine; chromosome(s), organelles, or membranes isolated from a cell; genomic DNA, RNA, or cDNA in solution or bound to a substrate; and cleared cells or tissues or blots or imprints from such cells or tissues).

[0113] “Specific binding” or “specifically binding” refers to the interaction between a protein or peptide and its agonist, antibody, antagonist, or other binding partner. The interaction is dependent upon the presence of a particular structure of the protein, e.g., the antigenic determinant or epitope, recognized by the binding molecule. For example, if an antibody is specific for epitope “A,” the presence of a polypeptide containing epitope A, or the presence of free unlabeled A, in a reaction containing free labeled A and the antibody will reduce the amount of labeled A that binds to the antibody.

[0114] “Substitution” refers to the replacement of at least one nucleotide or amino acid by a different nucleotide or amino acid.

[0115] “Substrate” refers to any suitable rigid or semi-rigid support including, e.g., membranes, filters, chips, slides, wafers, fibers, magnetic or nonmagnetic beads, gels, tubing, plates, polymers, microparticles or capillaries. The substrate can have a variety of surface forms, such as wells, trenches, pins, channels and pores, to which polynucleotides or polypeptides are bound.

[0116] A “transcript image” refers to the collective pattern of gene expression by a particular tissue or cell type under given conditions at a given time.

[0117] “Transformation” refers to a process by which exogenous DNA enters a recipient cell. Transformation may occur under natural or artificial conditions using various methods well known in the art. Transformation may rely on any known method for the insertion of foreign nucleic acid sequences into a prokaryotic or eukaryotic host cell. The method is selected based on the host cell being transformed.

[0118] “Transformants” include stably transformed cells in which the inserted DNA is capable of replication either as an autonomously replicating plasmid or as part of the host chromosome, as well as cells which transiently express inserted DNA or RNA.

[0119] A “transgenic organism,” as used herein, is any organism, including but not limited to animals and plants, in which one or more of the cells of the organism contains heterologous nucleic acid introduced by way of human intervention, such as by transgenic techniques well known in the art. The nucleic acid is introduced into the cell, directly or indirectly by introduced into a precursor of the cell, by way of deliberate genetic manipulation, such as by microinjection or by infection with a recombinant virus. The term genetic manipulation does not include classical cross-breeding, or in vitro fertilization, but rather is directed to the introduction of a recombinant DNA molecule. The transgenic organisms contemplated in accordance with the present invention include bacteria, cyanobacteria, fungi, and plants and animals. The isolated DNA of the present invention can be introduced into the host by methods known in the art, for example infection, transfection, transformation or transconjugation. Techniques for transferring the DNA of the present invention into such organisms are widely known and provided in references such as Sambrook et al. (1989), supra.

[0120] A “variant” of a particular nucleic acid sequence is defined as a nucleic acid sequence having at least 25% sequence identity to the particular nucleic acid sequence over a certain length of one of the nucleic acid sequences using blastn with the “BLAST 2 Sequences” tool Version 2.0.9 (May-07-1999) set at default parameters. Such a pair of nucleic acids may show, for example, at least 30%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or greater sequence identity over a certain defined length. The variant may result in “conservative” amino acid changes which do not affect structural and/or chemical properties. A variant may be described as, for example, an “allelic” (as defined above), “splice,” “species,” or “polymorphic” variant. A splice variant may have significant identity to a reference molecule, but will generally have a greater or lesser number of polynucleotides due to alternate splicing of exons during mRNA processing. The corresponding polypeptide may possess additional functional domains or lack domains that are present in the reference molecule. Species variants are polynucleotide sequences that vary from one species to another. The resulting polypeptides generally will have significant amino acid identity relative to each other. A polymorphic variant is a variation in the polynucleotide sequence of a particular gene between individuals of a given species. Polymorphic variants also may encompass “single nucleotide polymorphisms” (SNPs) in which the polynucleotide sequence varies by one base. The presence of SNPs may be indicative of, for example, a certain population, a disease state, or a propensity for a disease state.

[0121] In an alternative, variants of the polynucleotides of the present invention may be generated through recombinant methods. One possible method is a DNA shuffling technique such as MOLECULARBREEDING (Maxygen Inc., Santa Clara Calif.; described in U.S. Pat. No. 5,837,458; Chang, C. -C. et al. (1999) Nat. Biotechnol. 17:793-797; Christians, F. C. et al. (1999) Nat. Biotechnol. 17:259-264; and Crameri, A. et al. (1996) Nat. Biotechnol. 14:315-319) to alter or improve the biological properties of MDDT, such as its biological or enzymatic activity or its ability to bind to other molecules or compounds. DNA shuffling is a process by which a library of gene variants is produced using PCR-method recombination of gene fragments. The library is then subjected to selection or screening procedures that identify those gene variants with the desired properties. These preferred variants may then be pooled and further subjected to recursive rounds of DNA shuffling and selection/screening. Thus, genetic diversity is created through “artificial” breeding and rapid molecular evolution. For example, fragments of a single gene containing random point mutations may be recombined, screened, and then reshuffled until the desired properties are optimized. Alternatively, fragments of a given gene may be recombined with fragments of homologous genes in the same gene family, either from the same or different species, thereby maximizing the genetic diversity of multiple naturally occurring genes in a directed and controllable manner.

[0122] A “variant” of a particular polypeptide sequence is defined as a polypeptide sequence having at least 40% sequence identity to the particular polypeptide sequence over a certain length of one of the polypeptide sequences using blastp with the “BLAST 2 Sequences” tool Version 2.0.9 (May-07-1999) set at default parameters. Such a pair of polypeptides may show, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or greater sequence identity over a certain defined length of one of the polypeptides.

THE INVENTION

[0123] In a particular embodiment, cDNA sequences derived from human tissues and cell lines were aligned based on nucleotide sequence identity and assembled into “consensus” or “template” sequences which are designated by the template identification numbers (template IDs) in column 2 of Table 2. The sequence identification numbers (SEQ ID NO:s) corresponding to the template IDs are shown in column 1. The template sequences have similarity to GenBank sequences, or “hits,” as designated by the GI Numbers in column 3. The statistical probability of each GenBank hit is indicated by a probability score in column 4, and the functional annotation corresponding to each GenBank hit is listed in column 5.

[0124] The invention incorporates the nucleic acid sequences of these templates as disclosed in the Sequence Listing and the use of these sequences in the diagnosis and treatment of disease states characterized by defects in disease detection and treatment molecules. The invention further utilizes these sequences in hybridization and amplification technologies, and in particular, in technologies which assess gene expression patterns correlated with specific cells or tissues and their responses in vivo or in vitro to pharmaceutical agents, toxins, and other treatments. In this manner, the sequences of the present invention are used to develop a transcript image for a particular cell or tissue.

[0125] Derivation of Nucleic Acid Sequences

[0126] cDNA was isolated from libraries constructed using RNA derived from normal and diseased human tissues and cell lines. The human tissues and cell lines used for cDNA library construction were selected from a broad range of sources to provide a diverse population of cDNAs representative of gene transcription throughout the human body. Descriptions of the human tissues and cell lines used for cDNA library construction are provided in the LIFESEQ database (Incyte Genomics, Inc. (Incyte), Palo Alto Calif.). Human tissues were broadly selected from, for example, cardiovascular, dermatologic, endocrine, gastrointestinal, hematopoietic/immune system, musculoskeletal, neural, reproductive, and urologic sources.

[0127] Cell lines used for cDNA library construction were derived from, for example, leukemic cells, teratocarcinomas, neuroepitheliomas, cervical carcinoma, lung fibroblasts, and endothelial cells. Such cell lines include, for example, THP-1, Jurkat, HUVEC, hNT2, WI38, HeLa, and other cell lines commonly used and available from public depositories (American Type Culture Collection, Manassas Va.). Prior to mRNA isolation, cell lines were untreated, treated with a pharmaceutical agent such as 5′-aza-2′-deoxycytidine, treated with an activating agent such as lipopolysaccharide in the case of leukocytic cell lines, or, in the case of endothelial cell lines, subjected to shear stress.

[0128] Sequencing of the cDNAs

[0129] Methods for DNA sequencing are well known in the art. Conventional enzymatic methods employ the Klenow fragment of DNA polymerase I, SEQUENASE DNA polymerase (U.S. Biochemical Corporation, Cleveland Ohio), Taq polymerase (Applied Biosystems, Foster City Calif.), thermostable T7 polymerase (Amersham Pharmacia Biotech, Inc. (Amersham Pharmacia Biotech), Piscataway N.J.), or combinations of polymerases and proofreading exonucleases such as those found in the ELONGASE amplification system (Life Technologies Inc. (Life Technologies), Gaithersburg Md.), to extend the nucleic acid sequence from an oligonucleotide primer annealed to the DNA template of interest. Methods have been developed for the use of both single-stranded and double-stranded templates. Chain termination reaction products may be electrophoresed on urea-polyacrylamide gels and detected either by autoradiography (for radioisotope-labeled nucleotides) or by fluorescence (for fluorophore-labeled nucleotides). Automated methods for mechanized reaction preparation, sequencing, and analysis using fluorescence detection methods have been developed. Machines used to prepare cDNAs for sequencing can include the MICROLAB 2200 liquid transfer system (Hamilton Company (Hamilton), Reno Nev.), Peltier thermal cycler (PTC200; MJ Research, Inc. (MJ Research), Watertown Mass.), and ABI CATALYST 800 thermal cycler (Applied Biosystems). Sequencing can be carried out using, for example, the ABI 373 or 377 (Applied Biosystems) or MEGABACE 1000 (Molecular Dynamics, Inc. (Molecular Dynamics), Sunnyvale Calif.) DNA sequencing systems, or other automated and manual sequencing systems well known in the art.

[0130] The nucleotide sequences of the Sequence Listing have been prepared by current, state-of-the-art, automated methods and, as such, may contain occasional sequencing errors or unidentified nucleotides. Such unidentified nucleotides are designated by an N. These infrequent unidentified bases do not represent a hindrance to practicing the invention for those skilled in the art. Several methods employing standard recombinant techniques may be used to correct errors and complete the missing sequence information. (See, e.g., those described in Ausubel, F. M. et al. (1997) Short Protocols in Molecular Biology, John Wiley & Sons, New York N.Y.; and Sambrook, J. et al. (1989) Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Press, Plainview N.Y.)

[0131] Assembly of cDNA Sequences

[0132] Human polynucleotide sequences may be assembled using programs or algorithms well known in the art. Sequences to be assembled are related, wholly or in part, and may be derived from a single or many different transcripts. Assembly of the sequences can be performed using such programs as PHRAP (Phils Revised Assembly Program) and the GELVIEW fragment assembly system (GCG), or other methods known in the art.

[0133] Alternatively, cDNA sequences are used as “component” sequences that are assembled into “template” or “consensus” sequences as follows. Sequence chromatograms are processed, verified, and quality scores are obtained using PHRED. Raw sequences are edited using an editing pathway known as Block 1 (See, e.g., the LIFESEQ Assembled User Guide, Incyte Genomics, Palo Alto, Calif.). A series of BLAST comparisons is performed and low-information segments and repetitive elements (e.g., dinucleotide repeats, Alu repeats, etc.) are replaced by “n's”, or masked, to prevent spurious matches. Mitochondrial and ribosomal RNA sequences are also removed. The processed sequences are then loaded into a relational database management system (RDMS) which assigns edited sequences to existing templates, if available. When additional sequences are added into the RDMS, a process is initiated which modifies existing templates or creates new templates from works in progress (i.e., nonfinal assembled sequences) containing queued sequences or the sequences themselves. After the new sequences have been assigned to templates, the templates can be merged into bins. If multiple templates exist in one bin, the bin can be split and the templates reannotated.

[0134] Once gene bins have been generated based upon sequence alignments, bins are “clone joined” based upon clone information. Clone joining occurs when the 5′ sequence of one clone is present in one bin and the 3′ sequence from the same clone is present in a different bin, indicating that the two bins should be merged into a single bin. Only bins which share at least two different clones are merged.

[0135] A resultant template sequence may contain either a partial or a full length open reading frame, or all or part of a genetic regulatory element. This variation is due in part to the fact that the full length cDNAs of many genes are several hundred, and sometimes several thousand, bases in length. With current technology, cDNAs comprising the coding regions of large genes cannot be cloned because of vector limitations, incomplete reverse transcription of the mRNA, or incomplete “second strand” synthesis. Template sequences may be extended to include additional contiguous sequences derived from the parent RNA transcript using a variety of methods known to those of skill in the art. Extension may thus be used to achieve the full length coding sequence of a gene.

[0136] Analysis of the cDNA Sequences

[0137] The cDNA sequences are analyzed using a variety of programs and algorithms which are well known in the art. (See, e.g., Ausubel, 1997, supra, Chapter 7.7; Meyers, R. A. (Ed.) (1995) Molecular Biology and Biotechnology, Wiley VCH, New York N.Y., pp. 856-853; and Table 8.) These analyses comprise both reading frame determinations, e.g., based on triplet codon periodicity for particular organisms (Fickett, J. W. (1982) Nucleic Acids Res. 10:5303-5318); analyses of potential start and stop codons; and homology searches.

[0138] Computer programs known to those of skill in the art for performing computer-assisted searches for amino acid and nucleic acid sequence similarity, include, for example, Basic Local Alignment Search Tool (BLAST; Altschul, S. F. (1993) J. Mol. Evol. 36:290-300; Altschul, S. F. et al. (1990) J. Mol. Biol. 215:403-410). BLAST is especially useful in determining exact matches and comparing two sequence fragments of arbitrary but equal lengths, whose alignment is locally maximal and for which the alignment score meets or exceeds a threshold or cutoff score set by the user (Karlin, S. et al. (1988) Proc. Natl. Acad. Sci. USA 85:841-845). Using an appropriate search tool (e.g., BLAST or HMM), GenBank, SwissProt, BLOCKS, PFAM and other databases may be searched for sequences containing regions of homology to a query mddt or MDDT of the present invention.

[0139] Other approaches to the identification, assembly, storage, and display of nucleotide and polypeptide sequences are provided in “Relational Database for Storing Biomolecule Information,” U.S. Ser. No. 08/947,845, filed Oct. 9, 1997; “Project-Based Full-Length Biomolecular Sequence Database,” U.S. Ser. No. 08/811,758, filed Mar. 6, 1997; and “Relational Database and System for Storing Information Relating to Biomolecular Sequences,” U.S. Ser. No. 09/034,807, filed Mar. 4, 1998, all of which are incorporated by reference herein in their entirety.

[0140] Protein hierarchies can be assigned to the putative encoded polypeptide based on, e.g., motif, BLAST, or biological analysis. Methods for assigning these hierarchies are described, for example, in “Database System Employing Protein Function Hierarchies for Viewing Biomolecular Sequence Data,” U.S. Ser. No. 08/812,290, filed Mar. 6, 1997, incorporated herein by reference.

[0141] Human Disease Detection and Treatment Molecule Sequences

[0142] The mddt of the present invention may be used for a variety of diagnostic and therapeutic purposes. For example, an mddt may be used to diagnose a particular condition, disease, or disorder associated with disease detection and treatment molecules. Such conditions, diseases, and disorders include, but are not limited to, a cell proliferative disorder, such as actinic keratosis, arteriosclerosis, atherosclerosis, bursitis, cirrhosis, hepatitis, mixed connective tissue disease (MCTD), myelofibrosis, paroxysmal nocturnal hemoglobinuria, polycythemia vera, psoriasis, primary thrombocythemia, and cancers including adenocarcinoma, leukemia, lymphoma, melanoma, myeloma, sarcoma, teratocarcinoma, and, in particular, a cancer of the adrenal gland, bladder, bone, bone marrow, brain, breast, cervix, gall bladder, ganglia, gastrointestinal tract, heart, kidney, liver, lung, muscle, ovary, pancreas, parathyroid, penis, prostate, salivary glands, skin, spleen, testis, thymus, thyroid, and uterus; and an autoimmune/inflammatory disorder, such as actinic keratosis, acquired immunodeficiency syndrome (AIDS), Addison's disease, adult respiratory distress syndrome, allergies, ankylosing spondylitis, amyloidosis, anemia, arteriosclerosis, asthma, atherosclerosis, autoimmune hemolytic anemia, autoimmune thyroiditis, bronchitis, bursitis, cholecystitis, cirrhosis, contact dermatitis, Crohn's disease, atopic dermatitis, dermatomyositis, diabetes mellitus, emphysema, erythroblastosis fetalis, erythema nodosum, atrophic gastritis, glomerulonephritis, Goodpasture's syndrome, gout, Graves' disease, Hashimoto's thyroiditis, paroxysmal nocturnal hemoglobinuria, hepatitis, hypereosinophilia, irritable bowel syndrome, episodic lymphopenia with lymphocytotoxins, mixed connective tissue disease (MCTD), multiple sclerosis, myasthenia gravis, myocardial or pericardial inflammation, myelofibrosis, osteoarthritis, osteoporosis, pancreatitis, polycythemia vera, polymyositis, psoriasis, Reiter's syndrome, rheumatoid arthritis, scleroderma, Sjögren's syndrome, systemic anaphylaxis, systemic lupus erythematosus, systemic sclerosis, primary thrombocythemia, thrombocytopenic purpura, ulcerative colitis, uveitis. Werner syndrome, complications of cancer, hemodialysis, and extracorporeal circulation, trauma, and hematopoietic cancer including lymphoma, leukemia, and myeloma. The mddt can be used to detect the presence of, or to quantify the amount of, an mddt-related polynucleotide in a sample. This information is then compared to information obtained from appropriate reference samples, and a diagnosis is established. Alternatively, a polynucleotide complementary to a given mddt can inhibit or inactivate a therapeutically relevant gene related to the mddt.

[0143] Analysis of mddt Expression Patterns

[0144] The expression of mddt may be routinely assessed by hybridization-based methods to determine, for example, the tissue-specificity, disease-specificity, or developmental stage-specificity of mddt expression. For example, the level of expression of mddt may be prepared among different cell types or tissues, among diseased and normal cell types or tissues, among cell types or tissues at different developmental stages, or among cell types or tissues undergoing various treatments. This type of analysis is useful, for example, to assess the relative levels of mddt expression in fully or partially differentiated cells or tissues, to determine if changes in mddt expression levels are correlated with the development or progression of specific disease states, and to assess the response of a cell or tissue to a specific therapy, for example, in pharmacological or toxicological studies. Methods for the analysis of mddt expression are based on hybridization and amplification technologies and include membrane-based procedures such as northern blot analysis, high-throughput procedures that utilize, for example, microarrays, and PCR-based procedures.

[0145] Hybridization and Genetic Analysis

[0146] The mddt, their fragments, or complementary sequences, may be used to identify the presence of and/or to determine the degree of similarity between two (or more) nucleic acid sequences. The mddt may be hybridized to naturally occurring or recombinant nucleic acid sequences under appropriately selected temperatures and salt concentrations. Hybridization with a probe based on the nucleic acid sequence of at least one of the mddt allows for the detection of nucleic acid sequences, including genomic sequences, which are identical or related to the mddt of the Sequence Listing. Probes may be selected from non-conserved or unique regions of at least one of the polynucleotides of SEQ ID NO:1-252 and tested for their ability to identify or amplify the target nucleic acid sequence using standard protocols.

[0147] Polynucleotide sequences that are capable of hybridizing, in particular, to those shown in SEQ ID NO:1-252 and fragments thereof, can be identified using various conditions of stringency. (See, e.g., Wahl, G. M. and S. L. Berger (1987) Methods Enzymol. 152:399-407; Kimmel, A. R. (1987) Methods Enzymol. 152:507-511.) Hybridization conditions are discussed in “Definitions.”

[0148] A probe for use in Southern or northern hybridization may be derived from a fragment of an mddt sequence, or its complement, that is up to several hundred nucleotides in length and is either single-stranded or double-stranded. Such probes may be hybridized in solution to biological materials such as plasmids, bacterial, yeast, or human artificial chromosomes, cleared or sectioned tissues, or to artificial substrates containing mddt. Microarrays are particularly suitable for identifying the presence of and detecting the level of expression for multiple genes of interest by examining gene expression correlated with, e.g., various stages of development, treatment with a drug or compound, or disease progression. An array analogous to a dot or slot blot may be used to arrange and link polynucleotides to the surface of a substrate using one or more of the following: mechanical (vacuum), chemical, thermal, or UV bonding procedures. Such an array may contain any number of mddt and may be produced by hand or by

available devices, materials, and machines.

[0149] Microarrays may prepared, used, and analyzed using methods own in the art. (See, e.g., Brennan, T. M. et al. (1995) U.S. Pat. No. 5,474,796; Schena, M. et al. (1996) Proc. Natl. Acad. Sci. USA 93:10614-10619; Baldeschweiler et al. (1995) PCT application WO95/251116; Shalon, D. et al. (1995) PCT application WO95/35505; Heller, R. A. et al. (1997) Proc. Natl. Acad. Sci. USA 94:2150-2155; and Heller, M. J. et al. (1997) U.S. Pat. No. 5,605,662.)

[0150] Probes may be labeled by either PCR or enzymatic techniques using a variety of commercially available reporter molecules. For example, commercial kits are available for radioactive and chemiluminescent labeling (Amersham Pharmacia Biotech) and for alkaline phosphatase labeling (Life Technologies). Alternatively, mddt may be cloned into commercially available vectors for the production of RNA probes. Such probes may be transcribed in the presence of at least one labeled nucleotide (e.g., ³²P-ATP, Amersham Pharmacia Biotech).

[0151] Additionally the polynucleotides of SEQ ID NO:1-252 or suitable fragments thereof can be used to isolate full length cDNA sequences utilizing hybridization and/or amplification procedures well known in the art, e.g., cDNA library screening, PCR amplification, etc. The molecular cloning of such full length cDNA sequences may employ the method of cDNA library screening with probes using the hybridization, stringency, washing, and probing strategies described above and in Ausubel, supra, Chapters 3, 5, and 6. These procedures may also be employed with genomic libraries to isolate genomic sequences of mddt in order to analyze, e.g., regulatory elements.

[0152] Genetic Mapping

[0153] Gene identification and mapping are important in the investigation and treatment of almost all conditions, diseases, and disorders. Cancer, cardiovascular disease, Alzheimer's disease, arthritis, diabetes, and mental illnesses are of particular interest. Each of these conditions is more complex than the single gene defects of sickle cell anemia or cystic fibrosis, with select groups of genes being predictive of predisposition for a particular condition, disease, or disorder. For example, cardiovascular disease may result from malfunctioning receptor molecules that fail to clear cholesterol from the bloodstream, and diabetes may result when a particular individual's immune system is activated by an infection and attacks the insulin-producing cells of the pancreas. In some studies, Alzheimer's disease has been linked to a gene on chromosome 21; other studies predict a different gene and location. Mapping of disease genes is a complex and reiterative process and generally proceeds from genetic linkage analysis to physical mapping.

[0154] As a condition is noted among members of a family, a genetic linkage map traces parts of chromosomes that are inherited in the same pattern as the condition. Statistics link the inheritance of particular conditions to particular regions of chromosomes, as defined by RFLP or other markers. (See, for example, Lande

S. and Botstein, D. (1986) Proc. Natl. Acad. Sci. USA 83:7353-7357.) Occasionally, genetic markers and their locations are known from previous studies. More often, however, the markers are simply stretches of DNA that differ among individuals. Examples of genetic linkage maps can be found in various scientific journals or at the Online Mendelian Inheritance in Man (OMIM) World Wide Web site.

[0155] In another embodiment of the invention, mddt sequences may be used to generate hybridization probes useful in chromosomal mapping of naturally occurring genomic sequences. Either coding or noncoding sequences of mddt may be used, and in some instances, noncoding sequences may be preferable over coding sequences. For example, conservation of an mddt coding sequence among members of a multi-gene family may potentially cause undesired cross hybridization during chromosomal mapping. The sequences may be mapped to a particular chromosome, to a specific region of a chromosome, or to artificial chromosome constructions, e.g., human artificial chromosomes (HACs), yeast artificial chromosomes (YACs), bacterial artificial chromosomes (BACs), bacterial P1 constructions, or single chromosome cDNA libraries. (See, e.g., Harrington, J. J. et al. (1997) Nat. Genet. 15:345-355; Price, C. M. (1993) Blood Rev. 7:127-134; and Trask, B. J. (1991) Trends Genet. 7:149-154.)

[0156] Fluorescent in situ hybridization (FISH) may be correlated with other physical chromosome mapping techniques and genetic map data. (See, e.g., Meyers, supra, pp. 965-968.) Correlation between the location of mddt on a physical chromosomal map and a specific disorder, or a predisposition to a specific disorder, may help define the region of DNA associated with that disorder. The mddt sequences may also be used to detect polymorphisms that are genetically linked to the inheritance of a particular condition, disease, or disorder.

[0157] In situ hybridization of chromosomal preparations and genetic mapping techniques, such as linkage analysis using established chromosomal markers, may be used for extending existing genetic maps. Often the placement of a gene on the chromosome of another mammalian species, such as mouse, may reveal associated markers even if the number or arm of the corresponding human chromosome is not known. These new marker sequences can be mapped to human chromosomes and may provide valuable information to investigators searching for disease genes using positional cloning or other gene discovery techniques. Once a disease or syndrome has been crudely correlated by genetic linkage with a particular genomic region, e.g., ataxia-telangiectasia to 11q22-23, any sequences mapping to that area may represent associated or regulatory genes for further investigation. (See, e.g., Gatti, R. A. et al. (1988) Nature 336:577-580.) The nucleotide sequences of the subject invention may also be used to detect differences in chromosomal architecture due to translocation, inversion, etc., among normal, carrier, or affected individuals.

[0158] Once a disease-associated gene is mapped to a chromosomal region, the gene must be cloned in order to identify mutant or other alterations (e.g., translocations o

esions) that may be correlated with disease. This process requires a physical map of the chromosomal region containing the disease-gene of interest along with associated markers. A physical map is necessary for determining the nucleotide sequence of and order of marker genes on a particular chromosomal region. Physical mapping techniques are well known in the art and require the generation of overlapping sets of cloned DNA fragments from a particular organelle, chromosome, or genome. These clones are analyzed to reconstruct and catalog their order. Once the position of a marker is determined, the DNA from that region is obtained by consulting the catalog and selecting clones from that region. The gene of interest is located through positional cloning techniques using hybridization or similar methods.

[0159] Diagnostic Uses

[0160] The mddt of the present invention may be used to design probes useful in diagnostic assays. Such assays, well known to those skilled in the art, may be used to detect or confirm conditions, disorders, or diseases associated with abnormal levels of mddt expression. Labeled probes developed from mddt sequences are added to a sample under hybridizing conditions of desired stringency. In some instances, mddt, or fragments or oligonucleotides derived from mddt, may be used as primers in amplification steps prior to hybridization. The amount of hybridization complex formed is quantified and compared with standards for that cell or tissue. If mddt expression varies significantly from the standard, the assay indicates the presence of the condition, disorder, or disease. Qualitative or quantitative diagnostic methods may include northern, dot blot, or other membrane or dip-stick based technologies or multiple-sample format technologies such as PCR, enzyme-linked immunosorbent assay (ELISA)-like, pin, or chip-based assays.

[0161] The probes described above may also be used to monitor the progress of conditions, disorders, or diseases associated with abnormal levels of mddt expression, or to evaluate the efficacy of a particular therapeutic treatment. The candidate probe may be identified from the mddt that are specific to a given human tissue and have not been observed in GenBank or other genome databases. Such a probe may be used in animal studies, preclinical tests, clinical trials, or in monitoring the treatment of an individual patient. In a typical process, standard expression is established by methods well known in the art for use as a basis of comparison, samples from patients affected by the disorder or disease are combined with the probe to evaluate any deviation from the standard profile, and a therapeutic agent is administered and effects are monitored to generate a treatment profile. Efficacy is evaluated by determining whether the expression progresses toward or returns to the standard normal pattern. Treatment profiles may be generated over a period of several days or several months. Statistical methods well known to those skilled in the art may be use to determine the significance of such therapeutic agents.

[0162] The polynucleotides are also useful for identifying individuals from minute biological samples, for example, by matching the RFLP pattern of a sample's DNA to that of an individual's DNA. The polynucleotides of the present invention can also be used to determine the actual base-by-base DNA sequence of selected portions of an individual's genome. These sequences can be used to prepare PCR primers for amplifying and isolating such selected DNA, which can then be sequenced. Using this technique, an individual can be identified through a unique set of DNA sequences. Once a unique ID database is established for an individual, positive identification of that individual can be made from extremely small tissue samples.

[0163] In a particular aspect, oligonucleotide primers derived from the mddt of the invention may be used to detect single nucleotide polymorphisms (SNPs). SNPs are substitutions, insertions and deletions that are a frequent cause of inherited or acquired genetic disease in humans. Methods of SNP detection include, but are not limited to, single-stranded conformation polymorphism (SSCP) and fluorescent SSCP (fSSCP) methods. In SSCP, oligonucleotide primers derived from mddt are used to amplify DNA using the polymerase chain reaction (PCR). The DNA may be derived, for example, from diseased or normal tissue, biopsy samples, bodily fluids, and the like. SNPs in the DNA cause differences in the secondary and tertiary structures of PCR products in single-stranded form, and these differences are detectable using gel electrophoresis in non-denaturing gels. In fSCCP, the oligonucleotide primers are fluorescently labeled, which allows detection of the amplimers in high-throughput equipment such as DNA sequencing machines. Additionally, sequence database analysis methods, termed in silico SNP (is SNP), are capable of identifying polymorphisms by comparing the sequences of individual overlapping DNA fragments which assemble into a common consensus sequence. These computer-based methods filter out sequence variations due to laboratory preparation of DNA and sequencing errors using statistical models and automated analyses of DNA sequence chromatograms. In the alternative, SNPs may be detected and characterized by mass spectrometry using, for example, the high throughput MASSARRAY system (Sequenom, Inc., San Diego Calif.).

[0164] DNA-based identification techniques are critical in forensic technology. DNA sequences taken from very small biological samples such as tissues, e.g., hair or skin, or body fluids, e.g., blood, saliva, semen, etc., can be amplified using, e.g., PCR, to identify individuals. (See, e.g., Erlich, H. (1992) PCR Technology, Freeman and Co., New York, N.Y.). Similarly, polynucleotides of the present invention can be used as polymorphic markers.

[0165] There is also a need for reagents capable of identifying the source of a particular tissue. Appropriate reagents can comprise, for example, DNA probes or primers prepared from the sequences of the present invention that are specific for particular tissues. Panels of such reagents can identify tissue by species and/or by organ type. In a similar fashion, these reagents can be used to screen tissue cultures for examination.

[0166] The polynucleotides of the present invention can also be used as molecular weight markers on nucleic acid gels or Southern blots, as diagnostic probes for the presence of a specific mRNA in a particular cell type, in the creation of subtracted cDNA libraries which aid in the discovery of novel polynucleotides, in selection and synthesis of oligomers for attachment to an array or other support, and as an antigen to elicit an immune response.

[0167] Disease Model Systems Using mddt

[0168] The mddt of the invention or their mammalian homologs may be “knocked out” in an animal model system using homologous recombination in embryonic stem (ES) cells. Such techniques are well known in the art and are useful for the generation of animal models of human disease. (See, e.g., U.S. Pat. No. 5,175,383 and U.S. Pat. No. 5,767,337.) For example, mouse ES cells, such as the mouse 129/SvJ cell line, are derived from the early mouse embryo and grown in culture. The ES cells are transformed with a vector containing the gene of interest disrupted by a marker gene, e.g., the neomycin phosphotransferase gene (neo; Capecchi, M. R. (1989) Science 244:1288-1292). The vector integrates into the corresponding region of the host genome by homologous recombination. Alternatively, homologous recombination takes place using the Cre-loxP system to knockout a gene of interest in a tissue- or developmental stage-specific manner (Marth, J. D. (1996) Clin. Invest. 97:1999-2002; Wagner, K. U. et al. (1997) Nucleic Acids Res. 25:4323-4330). Transformed ES cells are identified and microinjected into mouse cell blastocysts such as those from the C57BL/6 mouse strain. The blastocysts are surgically transferred to pseudopregnant dams, and the resulting chimeric progeny are genotyped and bred to produce heterozygous or homozygous strains. Transgenic animals thus generated may be tested with potential therapeutic or toxic agents.

[0169] The mddt of the invention may also be manipulated in vitro in ES cells derived from human blastocysts. Human ES cells have the potential to differentiate into at least eight separate cell lineages including endoderm, mesoderm, and ectodermal cell types. These cell lineages differentiate into, for example, neural cells, hematopoietic lineages, and cardiomyocytes (Thomson, J. A. et al. (1998) Science 282:1145-1147).

[0170] The mddt of the invention can also be used to create “knockin” humanized animals (pigs) or transgenic animals (mice or rats) to model human disease. With knockin technology, a region of mddt is injected into animal ES cells, and the injected sequence integrates into the animal cell genome. Transformed cells are injected into blastulae, and the blastulae are implanted as described above. Transgenic progeny or inbred lines are studied and treated with potential pharmaceutical agents to obtain information on treatment of a human disease. Alternatively, a mammal inbred to overexpress mddt, resulting, e.g., in the secretion of MDDT in its milk, may also serve as a convenient source of that protein (Janne, J. et al. (1998) Biotechnol. Annu. Rev. 4:55-74).

[0171] Screening Assays

[0172] MDDT encoded by polynucleotides of the present invention may be used to screen for molecules that bind to or are bound by the encoded polypeptides. The binding of the polypeptide and the molecule may activate (agonist), increase, inhibit (antagonist), or decrease activity of the polypeptide or the bound molecule. Examples of such molecules include antibodies, oligonucleotides, proteins (e.g., receptors), or small molecules.

[0173] Preferably, the molecule is closely related to the natural ligand of the polypeptide, e.g., a ligand or fragment thereof, a natural substrate, or a structural or functional mimetic. (See, Coligan et al., (1991) Current Protocols in Immunology 1(2): Chapter 5.) Similarly, the molecule can be closely related to the natural receptor to which the polypeptide binds, or to at least a fragment of the receptor, e.g., the active site. In either case, the molecule can be rationally designed using known techniques. Preferably, the screening for these molecules involves producing appropriate cells which express the polypeptide, either as a secreted protein or on the cell membrane. Preferred cells include cells from mammals, yeast, Drosophila, or E. coli. Cells expressing the polypeptide or cell membrane fractions which contain the expressed polypeptide are then contacted with a test compound and binding, stimulation, or inhibition of activity of either the polypeptide or the molecule is analyzed.

[0174] An assay may simply test binding of a candidate compound to the polypeptide, wherein binding is detected by a fluorophore, radioisotope, enzyme conjugate, or other detectable label. Alternatively, the assay may assess binding in the presence of a labeled competitor.

[0175] Additionally, the assay can be carried out using cell-free preparations, polypeptide/molecule affixed to a solid support, chemical libraries, or natural product mixtures. The assay may also simply comprise the steps of mixing a candidate compound with a solution containing a polypeptide, measuring polypeptide/molecule activity or binding, and comparing the polypeptide/molecule activity or binding to a standard.

[0176] Preferably, an ELISA assay using, e.g., a monoclonal or polyclonal antibody, can measure polypeptide level in a sample. The antibody can measure polypeptide level by either binding, directly or indirectly, to the polypeptide or by competing with the polypeptide for a substrate.

[0177] All of the above assays can be used in a diagnostic or prognostic context. The molecules discovered using these assays can be used to treat disease or to bring about a particular result in a patient (e.g., blood vessel growth) by activating or inhibiting the polypeptide/molecule. Moreover, the assays can discover agents which may inhibit or enhance the production of the polypeptide from suitably manipulated cells or tissues.

[0178] Transcript Imaging and Toxicological Testing

[0179] Another embodiment relates to the use of mddt to develop a transcript image of a tissue or cell type. A transcript image represents the global pattern of gene expression by a particular tissue or cell type. Global gene expression patterns are analyzed by quantifying the number of expressed genes and their relative abundance under given conditions and at a given time. (See Seilhamer et al., “Comparative Gene Transcript Analysis,” U.S. Pat. No. 5,840,484, expressly incorporated by reference herein.) Thus a transcript image may be generated by hybridizing the polynucleotides of the present invention or their complements to the totality of transcripts or reverse transcripts of a particular tissue or cell type. In one embodiment, the hybridization takes place in high-throughput format, wherein the polynucleotides of the present invention or their complements comprise a subset of a plurality of elements on a microarray. The resultant transcript image would provide a profile of gene activity pertaining to disease detection and treatment molecules.

[0180] Transcript images which profile mddt expression may be generated using transcripts isolated from tissues, cell lines, biopsies, or other biological samples. The transcript image may thus reflect mddt expression in vivo, as in the case of a tissue or biopsy sample, or in vitro, as in the case of a cell line.

[0181] Transcript images which profile mddt expression may also be used in conjunction with in vitro model systems and preclinical evaluation of pharmaceuticals, as well as toxicological testing of industrial and naturally-occurring environmental compounds. All compounds induce characteristic gene expression patterns, frequently termed molecular fingerprints or toxicant signatures, which are indicative of mechanisms of action and toxicity (Nuwaysir, E. F. et al. (1999) Mol. Carcinog. 24:153-159; Steiner, S. and Anderson, N. L. (2000) Toxicol. Lett. 112-113:467-71, expressly incorporated by reference herein). If a test compound has a signature similar to that of a compound with known toxicity, it is likely to share those toxic properties. These fingerprints or signatures are most useful and refined when they contain expression information from a large number of genes and gene families. Ideally, a genome-wide measurement of expression provides the highest quality signature. Even genes whose expression is not altered by any tested compounds are important as well, as the levels of expression of these genes are used to normalize the rest of the expression data. The normalization procedure is useful for comparison of expression data after treatment with different compounds. While the assignment of gene function to elements of a toxicant signature aids in interpretation of toxicity mechanisms, knowledge of gene function is not necessary for the statistical matching of signatures which leads to prediction of toxicity. (See, for example, Press Release 00-02 from the National Institute of Environmental Health Sciences, released Feb. 29, 2000, available at http://www.niehs.nih.gov/oc/news/toxchip.htm.) Therefore, it is important and desirable in toxicological screening using toxicant signatures to include all expressed gene sequences.

[0182] In one embodiment, the toxicity of a test compound is assessed in treating a biological sample containing nucleic acids with the test compound. Nucleic acids that are expressed in the treated biological sample are hybridized with one or more probes specific to the polynucleotides of the present invention, so that transcript levels corresponding to the polynucleotides of the present invention may be quantified. The transcript levels in the treated biological sample are compared with levels in an untreated biological sample. Differences in the transcript levels between the two samples are indicative of a toxic response caused by the test compound in the treated sample.

[0183] Another particular embodiment relates to the use of MDDT encoded by polynucleotides of the present invention to analyze the proteome of a tissue or cell type. The term proteome refers to the global pattern of protein expression in a particular tissue or cell type. Each protein component of a proteome can be subjected individually to further analysis. Proteome expression patterns, or profiles, are analyzed by quantifying the number of expressed proteins and their relative abundance under given conditions and at a given time. A profile of a cell's proteome may thus be generated by separating and analyzing the polypeptides of a particular tissue or cell type. In one embodiment, the separation is achieved using two-dimensional gel electrophoresis, in which proteins from a sample are separated by isoelectric focusing in the first dimension, and then according to molecular weight by sodium dodecyl sulfate slab gel electrophoresis in the second dimension (Steiner and Anderson, supra). The proteins are visualized in the gel as discrete and uniquely positioned spots, typically by staining the gel with an agent such as Coomassie Blue or silver or fluorescent stains. The optical density of each protein spot is generally proportional to the level of the protein in the sample. The optical densities of equivalently positioned protein spots from different samples, for example, from biological samples either treated or untreated with a test compound or therapeutic agent, are compared to identify any changes in protein spot density related to the treatment. The proteins in the spots are partially sequenced using, for example, standard methods employing chemical or enzymatic cleavage followed by mass spectrometry. The identity of the protein in a spot may be determined by comparing its partial sequence, preferably of at least 5 contiguous amino acid residues, to the polypeptide sequences of the present invention. In some cases, further sequence data may be obtained for definitive protein identification.

[0184] A proteomic profile may also be generated using antibodies specific for MDDT to quantify the levels of MDDT expression. In one embodiment, the antibodies are used as elements on a microarray, and protein expression levels are quantified by exposing the microarray to the sample and detecting the levels of protein bound to each array element (Lueking, A. et al. (1999) Anal. Biochem. 270:103-11; Mendoze, L. G. et al. (1999) Biotechniques 27:778-88). Detection may be performed by a variety of methods known in the art, for example, by reacting the proteins in the sample with a thiol- or amino-reactive fluorescent compound and detecting the amount of fluorescence bound at each array element.

[0185] Toxicant signatures at the proteome level are also useful for toxicological screening, and should be analyzed in parallel with toxicant signatures at the transcript level. There is a poor correlation between transcript and protein abundances for some proteins in some tissues (Anderson. N. L. and Seilhamer, J. (1997) Electrophoresis 18:533-537), so proteome toxicant signatures may be useful in the analysis of compounds which do not significantly affect the transcript image, but which alter the proteomic profile. In addition, the analysis of transcripts in body fluids is difficult, due to rapid degradation of mRNA, so proteomic profiling may be more reliable and informative in such cases.

[0186] In another embodiment, the toxicity of a test compound is assessed by treating a biological sample containing proteins with the test compound. Proteins that are expressed in the treated biological sample are separated so that the amount of each protein can be quantified. The amount of each protein is compared to the amount of the corresponding protein in an untreated biological sample. A difference in the amount of protein between the two samples is indicative of a toxic response to the test compound in the treated sample. Individual proteins are identified by sequencing the amino acid residues of the individual proteins and comparing these partial sequences to the MDDT encoded by polynucleotides of the present invention.

[0187] In another embodiment, the toxicity of a test compound is assessed by treating a biological sample containing proteins with the test compound. Proteins from the biological sample are incubated with antibodies specific to the MDDT encoded by polynucleotides of the present invention. The amount of protein recognized by the antibodies is quantified. The amount of protein in the treated biological sample is compared with the amount in an untreated biological sample. A difference in the amount of protein between the two samples is indicative of a toxic response to the test compound in the treated sample.

[0188] Transcript images may be used to profile mddt expression in distinct tissue types. This process can be used to determine disease detection and treatment molecule activity in a particular tissue type relative to this activity in a different tissue type. Transcript images may be used to generate a profile of mddt expression characteristic of diseased tissue. Transcript images of tissues before and after treatment may be used for diagnostic purposes, to monitor the progression of disease, and to monitor the efficacy of drug treatments for diseases which affect the activity of disease detection and treatment molecules.

[0189] Transcript images of cell lines can be used to assess disease detection and treatment molecule activity and/or to identify cell lines that lack or misregulate this activity. Such cell lines may then be treated with pharmaceutical agents, and a transcript image following treatment may indicate the efficacy of these agents in restoring desired levels of this activity. A similar approach may be used to assess the toxicity of pharmaceutical agents as reflected by undesirable changes in disease detection and treatment molecule

ity. Candidate pharmaceutical agents may be evaluated by comparing their associated transcript images with those of pharmaceutical agents of known effectiveness.

[0190] Antisense Molecules

[0191] The polynucleotides of the present invention are useful in antisense technology. Antisense technology or therapy relies on the modulation of expression of a target protein through the specific binding of an antisense sequence to a target sequence encoding the target protein or directing its expression. (See, e.g., Agrawal, S., ed. (1996) Antisense Therapeutics, Humana Press Inc. Totawa N.J.; Alama, A. et al. (1997) Pharmacol. Res. 36(3): 171-178; Crooke, S. T. (1997) Adv. Pharmacol. 40:1-49; Sharma, H. W. and R. Narayanan (1995) Bioessays 17(12):1055-1063; and Lavrosky, Y. et al. (1997) Biochem. Mol. Med. 62(1):11-22.) An antisense sequence is a polynucleotide sequence capable of specifically hybridizing to at least a portion of the target sequence. Antisense sequences bind to cellular mRNA and/or genomic DNA, affecting translation and/or transcription. Antisense sequences can be DNA, RNA, or nucleic acid mimics and analogs. (See, e.g., Rossi, J. J. et al. (1991) Antisense Res. Dev. 1(3):285-288; Lee, R. et al. (1998) Biochemistry 37(3):900-1010; Pardridge, W. M. et al. (1995) Proc. Natl. Acad. Sci. USA 92(12):5592-5596; and Nielsen, P. E. and Haaima, G. (1997) Chem. Soc. Rev. 96:73-78.) Typically, the binding which results in modulation of expression occurs through hybridization or binding of complementary base pairs. Antisense sequences can also bind to DNA duplexes through specific interactions in the major groove of the double helix.

[0192] The polynucleotides of the present invention and fragments thereof can be used as antisense sequences to modify the expression of the polypeptide encoded by mddt. The antisense sequences can be produced ex vivo, such as by using any of the ABI nucleic acid synthesizer series (Applied Biosystems) or other automated systems known in the art. Antisense sequences can also be produced biologically, such as by transforming an appropriate host cell with an expression vector containing the sequence of interest. (See, e.g., Agrawal, supra.)

[0193] In therapeutic use, any gene delivery system suitable for introduction of the antisense sequences into appropriate target cells can be used. Antisense sequences can be delivered intracellularly in the form of an expression plasmid which, upon transcription, produces a sequence complementary to at least a portion of the cellular sequence encoding the target protein. (See, e.g., Slater, J. E., et al. (1998) J. Allergy Clin. Immunol. 102(3):469-475; and Scanlon, K. J., et al. (1995) 9(13): 1288-1296.) Antisense sequences can also be introduced intracellularly through the use of viral vectors, such as retrovirus and adeno-associated virus vectors. (See, e.g., Miller, A. D. (1990) Blood 76:271; Ausubel, F. M. et al. (1995) Current Protocols in Molecular Biology, John Wiley & Sons, New York N.Y.; Uckert, W. and W. Walther (1994) Pharmacol. Ther. 63(3):323-347.) Other gene delivery mechanisms include liposome-derived systems, artificial viral envelopes, and other systems known in the art. (See, e.g., Rossi,

1995) Br. Med. Bull. 51(1):217-225; Boa

J. et al. (1998) J. Pharm. Sci. 87(11):1308-1315; and Morris, M. C. et al. (1997) Nucleic Acids Res. 25(14):2730-2736.)

[0194] Expression

[0195] In order to express a biologically active MDDT, the nucleotide sequences encoding MDDT or fragments thereof may be inserted into an appropriate expression vector. i.e., a vector which contains the necessary elements for transcriptional and translational control of the inserted coding sequence in a suitable host. Methods which are well known to those skilled in the art may be used to construct expression vectors containing sequences encoding MDDT and appropriate transcriptional and translational control elements. These methods include in vitro recombinant DNA techniques, synthetic techniques, and in vivo genetic recombination. (See, e.g., Sambrook, supra, Chapters 4, 8, 16, and 17; and Ausubel, supra, Chapters 9, 10, 13, and 16.)

[0196] A variety of expression vector/host systems may be utilized to contain and express sequences encoding MDDT. These include, but are not limited to, microorganisms such as bacteria transformed with recombinant bacteriophage, plasmid, or cosmid DNA expression vectors; yeast transformed with yeast expression vectors; insect cell systems infected with viral expression vectors (e.g., baculovirus); plant cell systems transformed with viral expression vectors (e.g., cauliflower mosaic virus, CaMV, or tobacco mosaic virus, TMV) or with bacterial expression vectors (e.g., Ti or pBR322 plasmids); or animal (mammalian) cell systems. (See, e.g., Sambrook, supra; Ausubel, 1995, supra, Van Heeke, G. and S. M. Schuster (1989) J. Biol. Chem. 264:5503-5509; Bitter, G. A. et al. (1987) Methods Enzymol. 153:516-544; Scorer, C. A. et al. (1994) Bio/Technology 12:181-184; Engelhard, E. K. et al. (1994) Proc. Natl. Acad. Sci. USA 91:3224-3227; Sandig, V. et al. (1996) Hum. Gene Ther. 7:1937-1945; Takamatsu, N. (1987) EMBO J. 6:307-311; Coruzzi, G. et al. (1984) EMBO J. 3:1671-1680; Broglie, R. et al. (1984) Science 224:838-843; Winter, J. et al. (1991) Results Probl. Cell Differ. 17:85-105; The McGraw Hill Yearbook of Science and Technology (1992) McGraw Hill, New York N.Y., pp. 191-196; Logan, J. and T. Shenk (1984) Proc. Natl. Acad. Sci. USA 81:3655-3659; and Harrington, J. J. et al. (1997) Nat. Genet. 15:345-355.) Expression vectors derived from retroviruses, adenoviruses, or herpes or vaccinia viruses, or from various bacterial plasmids, may be used for delivery of nucleotide sequences to the targeted organ, tissue, or cell population. (See, e.g., Di Nicola, M. et al. (1998) Cancer Gen. Ther. 5(6):350-356: Yu, M. et al., (1993) Proc. Natl. Acad. Sci. USA 90(13):6340-6344; Buller, R. M. et al. (1985) Nature 317(6040):813-815; McGregor, D. P. et al. (1994) Mol. Immunol. 31(3):219-226; and Verma, I. M. and N. Somia (1997) Nature 389:239-242.) The invention is not limited by the host cell employed.

[0197] For long term production of recombinant proteins in mammalian systems, stable expression of MDDT in cell lines is preferred. For example, sequences encoding MDDT can be transformed into cell lines using expression vectors which may contain viral origins of relation and/or endogenous expression elements and a selectable marker gene on the same or on a separate vector. Any number of selection systems may be used to recover transformed cell lines. (See, e.g., Wigler, M. et al. (1977) Cell 11:223-232; Lowy, I. et al. (1980) Cell 22:817-823.; Wigler, M. et al. (1980) Proc. Natl. Acad. Sci. USA 77:3567-3570; Colbere-Garapin, F. et al. (1981) J. Mol. Biol. 150:1-14; Hartman, S. C. and R. C. Mulligan (1988) Proc. Natl. Acad. Sci. USA 85:8047-8051; Rhodes, C. A. (1995) Methods Mol. Biol. 55:121-131.)

[0198] Therapeutic Uses of mddt

[0199] The mddt of the invention may be used for somatic or germline gene therapy. Gene therapy may be performed to (i) correct a genetic deficiency (e.g., in the cases of severe combined immunodeficiency (SCID)-X1 disease characterized by X-linked inheritance (Cavazzana-Calvo, M. et al. (2000) Science 288:669-672), severe combined immunodeficiency syndrome associated with an inherited adenosine deaminase (ADA) deficiency (Blaese, R. M. et al. (1995) Science 270:475-480; Bordignon, C. et al. (1995) Science 270:470-475), cystic fibrosis (Zabner, J. et al. (1993) Cell 75:207-216; Crystal, R. G. et al. (1995) Hum. Gene Therapy 6:643-666; Crystal, R. G. et al. (1995) Hum. Gene Therapy 6:667-703), thalassemias, familial hypercholesterolemia, and hemophilia resulting from Factor VIII or Factor IX deficiencies (Crystal, R. G. (1995) Science 270:404-410; Verma, I. M. and Somia, N. (1997) Nature 389:239-242)), (ii) express a conditionally lethal gene product (e.g., in the case of cancers which result from unregulated cell proliferation), or (iii) express a protein which affords protection against intracellular parasites (e.g., against human retroviruses, such as human immunodeficiency virus (HIV) (Baltimore. D. (1988) Nature 335:395-396; Poeschla, E. et al. (1996) Proc. Natl. Acad. Sci. USA. 93:11395-11399), hepatitis B or C virus (HBV, HCV); fungal parasites, such as Candida albicans and Paracoccidioides brasiliensis; and protozoan parasites such as Plasmodium falciparum and Trypanosoma cruzi). In the case where a genetic deficiency in mddt expression or regulation causes disease, the expression of mddt from an appropriate population of transduced cells may alleviate the clinical manifestations caused by the genetic deficiency.

[0200] In a further embodiment of the invention, diseases or disorders caused by deficiencies in mddt are treated by constructing mammalian expression vectors comprising mddt and introducing these vectors by mechanical means into mddt-deficient cells. Mechanical transfer technologies for use with cells in vivo or ex vitro include (i) direct DNA microinjection into individual cells, (ii) ballistic gold particle delivery, (iii) liposome-mediated transfection, (iv) receptor-mediated gene transfer, and (v) the use of DNA transposons (Morgan, R. A. and Anderson, W. F. (1993) Annu. Rev. Biochem. 62:191-217; Ivics, Z. (1997) Cell 91:501-510; Boulay, J-L. and Récipon, H. (1998) Curr. Opin. Biotechnol. 9:445-450).

[0201] Expression vector that may be effective for the expression of may include, but are not limited to, the PCDNA 3.1, EPITAG, PRCCMV2, PREP, PVAX vectors (Invitrogen, Carlsbad Calif.). PCMV-SCRIPT, PCMV-TAG, PEGSH/PERV (Stratagene, La Jolla Calif.), and PTET-OFF, PTET-ON, PTRE2, PTRE2-LUC, PTK-HYG (Clontech. Palo Alto Calif.). The mddt of the invention may be expressed using (i) a constitutively active promoter, (e.g., from cytomegalovirus (CMV), Rous sarcoma virus (RSV), SV40 virus, thymidine kinase (TK), or β-actin genes), (ii) an inducible promoter (e.g., the tetracycline-regulated promoter (Gossen, M. and Bujard, H. (1992) Proc. Natl. Acad. Sci. U.S.A. 89:5547-5551; Gossen, M. et al., (1995) Science 268:1766-1769; Rossi, F. M. V. and Blau, H. M. (1998) Curr. Opin. Biotechnol. 9:451-456), commercially available in the T-REX plasmid (Invitrogen); the ecdysone-inducible promoter (available in the plasmids PVGRXR and PIND: Invitrogen); the FK506/rapamycin inducible promoter; or the RU486/mifepristone inducible promoter (Rossi, F. M. V. and Blau, H. M. supra), or (iii) a tissue-specific promoter or the native promoter of the endogenous gene encoding MDDT from a normal individual.

[0202] Commercially available liposome transformation kits (e.g., the PERFECT LIPID TRANSFECTION KIT, available from Invitrogen) allow one with ordinary skill in the art to deliver polynucleotides to target cells in culture and require minimal effort to optimize experimental parameters. In the alternative, transformation is performed using the calcium phosphate method (Graham, F. L. and Eb, A. J. (1973) Virology 52:456-467), or by electroporation (Neumann, E. et al. (1982) EMBO J. 1:841-845). The introduction of DNA to primary cells requires modification of these standardized mammalian transfection protocols.

[0203] In another embodiment of the invention, diseases or disorders caused by genetic defects with respect to mddt expression are treated by constructing a retrovirus vector consisting of (i) mddt under the control of an independent promoter or the retrovirus long terminal repeat (LTR) promoter, (ii) appropriate RNA packaging signals, and (iii) a Rev-responsive element (RRE) along with additional retrovirus cis-acting RNA sequences and coding sequences required for efficient vector propagation. Retrovirus vectors (e.g., PFB and PFBNEO) are commercially available (Stratagene) and are based on published data (Riviere, I. et al. (1995) Proc. Natl. Acad. Sci. U.S.A. 92:6733-6737), incorporated by reference herein. The vector is propagated in an appropriate vector producing cell line (VPCL) that expresses an envelope gene with a tropism for receptors on the target cells or a promiscuous envelope protein such as VSVg (Armentano, D. et al. (1987) J. Virol. 61:1647-1650; Bender, M. A. et al. (1987) J. Virol. 61:1639-1646; Adam, M. A. and Miller, A. D. (1988) J. Virol. 62:3802-3806; Dull, T. et al. (1998) J. Virol. 72:8463-8471; Zufferey, R. et al. (1998) J. Virol. 72:9873-9880). U.S. Pat. No. 5,910,434 to Rigg (“Method for obtaining retrovirus packaging cell lines producing high transducing efficiency retroviral supernatant”) discloses a method for obtaining retrovirus packaging cell lines and is hereby incorporated by reference. Propagation of retrovirus vectors, transduction of a population of cells (e.g. CD4⁺T-cells), and the return of transduced

to a patient are procedures well known to persons skilled in the art of gene therapy and have been well documented (Ranga, U. et al. (1997) J. Virol. 71:7020-7029; Bauer, G. et al. (1997) Blood 89:2259-2267; Bonyhadi, M. L. (1997) J. Virol. 71:47074716; Ranga, U. et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95:1201-1206; Su, L. (1997) Blood 89:2283-2290).

[0204] In the alternative, an adenovirus-based gene therapy delivery system is used to deliver mddt to cells which have one or more genetic abnormalities with respect to the expression of mddt. The construction and packaging of adenovirus-based vectors are well known to those with ordinary skill in the art. Replication defective adenovirus vectors have proven to be versatile for importing genes encoding immunoregulatory proteins into intact islets in the pancreas (Csete, M. E. et al. (1995) Transplantation 27:263-268). Potentially useful adenoviral vectors are described in U.S. Pat. No. 5,707,618 to Armentano (“Adenovirus vectors for gene therapy”), hereby incorporated by reference. For adenoviral vectors, see also Antinozzi, P. A. et al. (1999) Annu. Rev. Nutr. 19:511-544 and Verma, I. M. and Somia, N. (1997) Nature 18:389:239-242, both incorporated by reference herein.

[0205] In another alternative, a herpes-based, gene therapy delivery system is used to deliver mddt to target cells which have one or more genetic abnormalities with respect to the expression of mddt. The use of herpes simplex virus (HSV)-based vectors may be especially valuable for introducing mddt to cells of the central nervous system, for which HSV has a tropism. The construction and packaging of herpes-based vectors are well known to those with ordinary skill in the art. A replication-competent herpes simplex virus (HSV) type 1-based vector has been used to deliver a reporter gene to the eyes of primates (Liu, X. et al. (1999) Exp. Eye Res. 169:385-395). The construction of a HSV-1 virus vector has also been disclosed in detail in U.S. Pat. No. 5,804,413 to DeLuca (“Herpes simplex virus strains for gene transfer”), which is hereby incorporated by reference. U.S. Pat. No. 5,804,413 teaches the use of recombinant HSV d92 which consists of a genome containing at least one exogenous gene to be transferred to a cell under the control of the appropriate promoter for purposes including human gene therapy. Also taught by this patent are the construction and use of recombinant HSV strains deleted for ICP4, ICP27 and ICP22. For HSV vectors, see also Goins, W. F. et al. 1999 J. Virol. 73:519-532 and Xu, H. et al., (1994) Dev. Biol. 163:152-161, hereby incorporated by reference. The manipulation of cloned herpesvirus sequences, the generation of recombinant virus following the transfection of multiple plasmids containing different segments of the large herpesvirus genomes, the growth and propagation of herpesvirus, and the infection of cells with herpesvirus are techniques well known to those of ordinary skill in the art.

[0206] In another alternative, an alphavirus (positive, single-stranded RNA virus) vector is used to deliver mddt to target cells. The biology of the prototypic alphavirus, Semliki Forest Virus (SFV), has been studied extensively and gene transfer vectors have been based on the SFV genome (Garoff, H. and Li, K-J. (1998) Current Biotech. 9:464-469). During alphavirus RNA replication, a subgenomic RNA is generated that normally encodes the viral capsid proteins. This subgenomic RNA replicates to higher levels than the full-length genomic RNA, resulting in the overproduction of capsid proteins relative to the viral proteins with enzymatic activity (e.g., protease and polymerase). Similarly, inserting mddt into the alphavirus genome in place of the capsid-coding region results in the production of a large number of mddt RNAs and the synthesis of high levels of MDDT in vector transduced cells. While alphavirus infection is typically associated with cell lysis within a few days, the ability to establish a persistent infection in hamster normal kidney cells (BHK-21) with a variant of Sindbis virus (SIN) indicates that the lytic replication of alphaviruses can be altered to suit the needs of the gene therapy application (Dryga, S. A. et al. (1997) Virology 228:74-83). The wide host range of alphaviruses will allow the introduction of mddt into a variety of cell types. The specific transduction of a subset of cells in a population may require the sorting of cells prior to transduction. The methods of manipulating infectious cDNA clones of alphaviruses, performing alphavirus cDNA and RNA transfections, and performing alphavirus infections, are well known to those with ordinary skill in the art.

[0207] Antibodies

[0208] Anti-MDDT antibodies may be used to analyze protein expression levels. Such antibodies include, but are not limited to, polyclonal, monoclonal, chimeric, single chain, and Fab fragments. For descriptions of and protocols of antibody technologies, see, e.g., Pound J. D. (1998) Immunochemical Protocols, Humana Press, Totowa, N.J.

[0209] The amino acid sequence encoded by the mddt of the Sequence Listing may be analyzed by appropriate software (e.g., LASERGENE NAVIGATOR software, DNASTAR) to determine regions of high immunogenicity. The optimal sequences for immunization are selected from the C-terminus, the N-terminus, and those intervening, hydrophilic regions of the polypeptide which are likely to be exposed to the external environment when the polypeptide is in its natural conformation. Analysis used to select appropriate epitopes is also described by Ausubel (1997, supra, Chapter 11.7). Peptides used for antibody induction do not need to have biological activity; however, they must be antigenic. Peptides used to induce specific antibodies may have an amino acid sequence consisting of at least five amino acids, preferably at least 10 amino acids, and most preferably at least 15 amino acids. A peptide which mimics an antigenic fragment of the natural polypeptide may be fused with another protein such as keyhole hemolimpet cyanin (KLH; Sigma, St. Louis Mo.) for antibody production. A peptide encompassing an antigenic region may be expressed from an mddt, synthesized as described above, or purified from human cells.

[0210] Procedures well known in the art may be used for the production of antibodies. Various hosts including mice, goats, and rabbits, may be immunized by injection with peptide. Depending on the host species, various adjuvants may be used to increase immunological response.

[0211] In one procedure, peptides about 15 residues in length may be synthesized using an ABI 431 A peptide synthesizer (Applied Biosystems) using fmoc-chemistry and coupled to KLH (Sigma) by reaction with M-maleimidobenzoyl-N-hydroxysuccinimide ester (Ausubel, 1995, supra). Rabbits are immunized with the peptide-KLH complex in complete Freund's adjuvant. The resulting antisera are tested for antipeptide activity by binding the peptide to plastic, blocking with 1% bovine serum albumin (BSA), reacting with rabbit antisera, washing, and reacting with radioiodinated goat anti-rabbit IgG. Antisera with antipeptide activity are tested for anti-MDDT activity using protocols well known in the art, including ELISA, radioimmunoassay (RIA), and immunoblotting.

[0212] In another procedure, isolated and purified peptide may be used to immunize mice (about 100 μg of peptide) or rabbits (about 1 mg of peptide). Subsequently, the peptide is radioiodinated and used to screen the immunized animals' B-lymphocytes for production of antipeptide antibodies. Positive cells are then used to produce hybridomas using standard techniques. About 20 mg of peptide is sufficient for labeling and screening several thousand clones. Hybridomas of interest are detected by screening with radioiodinated peptide to identify those fusions producing peptide-specific monoclonal antibody. In a typical protocol, wells of a multi-well plate (FAST, Becton-Dickinson, Palo Alto, Calif.) are coated with affinity-purified, specific rabbit-anti-mouse (or suitable anti-species IgG) antibodies at 10 mg/ml. The coated wells are blocked with 1% BSA and washed and exposed to supernatants from hybridomas. After incubation, the wells are exposed to radiolabeled peptide at 1 mg/ml.

[0213] Clones producing antibodies bind a quantity of labeled peptide that is detectable above background. Such clones are expanded and subjected to 2 cycles of cloning. Cloned hybridomas are injected into pristane-treated mice to produce ascites, and monoclonal antibody is purified from the ascitic fluid by affinity chromatography on protein A (Amersham Pharmacia Biotech). Several procedures for the production of monoclonal antibodies, including in vitro production, are described in Pound (supra). Monoclonal antibodies with antipeptide activity are tested for anti-MDDT activity using protocols well known in the art, including ELISA, RIA, and immunoblotting.

[0214] Antibody fragments containing specific binding sites for an epitope may also be generated. For example, such fragments include, but are not limited to, the F(ab′)₂ fragments produced by pepsin digestion of the antibody molecule, and the Fab fragments generated by reducing the disulfide bridges of the F(ab′)₂ fragments. Alternatively, construction of Fab expression libraries in filamentous bacteriophage allows rapid and easy identification of monoclonal fragments with desired specificity (Pound, supra, Chaps. 45-47). Antibodies generated against polypeptide encoded by mddt can be used to purify and characterize full-length MDDT protein and its activity, binding partners, etc.

[0215] Assays Using Antibodies

[0216] Anti-MDDT antibodies may be used in assays to quantify the amount of MDDT found in a particular human cell. Such assays include methods utilizing the antibody and a label to detect expression level under normal or disease conditions. The peptides and antibodies of the invention may be used with or without modification or labeled by joining them, either covalently or noncovalently, with a reporter molecule.

[0217] Protocols for detecting and measuring protein expression using either polyclonal or monoclonal antibodies are well known in the art. Examples include ELISA, RIA, and fluorescent activated cell sorting (FACS). Such immunoassays typically involve the formation of complexes between the MDDT and its specific antibody and the measurement of such complexes. These and other assays are described in Pound (supra).

[0218] Without further elaboration, it is believed that one skilled in the art can, using the preceding description, utilize the present invention to its fullest extent. The following preferred specific embodiments are, therefore, to be construed as merely illustrative, and not limitative of the remainder of the disclosure in any way whatsoever.

[0219] The disclosures of all patents, applications, and publications mentioned above and below, including U.S. Serial No. 60/230,517, U.S. Serial No. 60/230,599, U.S. Serial No. 60/230,514, U.S. Serial No. 60/231,167, U.S. Serial No. 60/230,598, U.S. Serial No. 60/230,988, U.S. Serial No. 60/230,518, U.S. Serial No. 60/230,515, U.S. Serial No. 60/229,751, U.S. Serial No. 60/230,610, U.S. Serial No. 60/229,749, U.S. Serial No. 60/229,750, U.S. Serial No. 60/230,597, U.S. Serial No. 60/230,505, U.S. Serial No. 60/231,163, U.S. Serial No. 60/229,747, U.S. Serial No. 60/229,748, U.S. Serial No. 60/230,583, U.S. Serial No. 60/230,519, U.S. Serial No. 60/230,595, U.S. Serial No. 60/230,865, U.S. Serial No. 60/230,989, and U.S. Serial No. 60/230,951, are hereby expressly incorporated by reference.

EXAMPLES

[0220] I. Construction of cDNA Libraries

[0221] RNA was purchased from CLONTECH Laboratories, Inc. (Palo Alto Calif.) or isolated from various tissues. Some tissues were homogenized and lysed in guanidinium isothiocyanate, while others were homogenized and lysed in phenol or in a suitable mixture of denaturants, such as TRIZOL (Life Technologies), a monophasic solution of phenol and guanidine isothiocyanate. The resulting lysates were centrifuged over CsCl cushions or extracted with chloroform. RNA was precipitated with either isopropanol or sodium acetate and ethanol, or by other routine methods.

[0222] Phenol extraction and precipitation of RNA were repeated as necessary to increase RNA purity. In most cases. RNA was treated with DNase. For most libraries, poly(A+) RNA was isolated using oligo d(T)coupled

magnetic particles (Promega Corporation, Omega), Madison Wis.), OLIGOTEX latex particles (QIAGEN, Inc. (QIAGEN), Valencia Calif.), or an OLIGOTEX mRNA purification kit (QIAGEN). Alternatively, RNA was isolated directly from tissue lysates using other RNA isolation kits, e.g., the POLY(A)PURE mRNA purification kit (Ambion, Inc. Austin Tex.).

[0223] In some cases, Stratagene was provided with RNA and constructed the corresponding cDNA libraries. Otherwise, cDNA was synthesized and cDNA libraries were constructed with the UNIZAP vector system (Stratagene Cloning Systems, Inc. (Stratagene), La Jolla Calif.) or SUPERSCRIPT plasmid system (Life Technologies), using the recommended procedures or similar methods known in the art. (See, e.g., Ausubel, 1997, supra, Chapters 5.1 through 6.6.) Reverse transcription was initiated using oligo d(T) or random primers. Synthetic oligonucleotide adapters were ligated to double stranded cDNA, and the cDNA was digested with the appropriate restriction enzyme or enzymes. For most libraries, the cDNA was size-selected (300-1000 bp) using SEPHACRYL S1000, SEPHAROSE CL2B, or SEPHAROSE CL4B column chromatography (Amersham Pharmacia Biotech) or preparative agarose gel electrophoresis. cDNAs were ligated into compatible restriction enzyme sites of the polylinker of a suitable plasmid, e.g. PBLUESCRIPT plasmid (Stratagene), PSPORT1 plasmid (Life Technologies), PCDNA2.1 plasmid (Invitrogen, Carlsbad Calif.), PBK-CMV plasmid (Stratagene), or pINCY (Incyte Genomics, Palo Alto Calif.), or derivatives thereof. Recombinant plasmids were transformed into competent E. coli cells including XL1-Blue, XL1-BlueMRF, or SOLR from Stratagene or DH5α, DH10B, or ElectroMAX DH10B from Life Technologies.

[0224] II. Isolation of cDNA Clones

[0225] Plasmids were recovered from host cells by in vivo excision using the UNIZAP vector system (Stratagene) or by cell lysis. Plasmids were purified using at least one of the following: the Magic or WIZARD Minipreps DNA purification system (Promega); the AGTC Miniprep purification kit (Edge BioSystems, Gaithersburg Md.); and the QIAWELL 8, QIAWELL 8 Plus, and QIAWELL 8 Ultra plasmid purification systems or the R.E.A.L. PREP 96 plasmid purification kit (QIAGEN). Following precipitation, plasmids were resuspended in 0.1 ml of distilled water and stored, with or without lyophilization, at 4° C.

[0226] Alternatively, plasmid DNA was amplified from host cell lysates using direct link PCR in a high-throughput format. (Rao, V. B. (1994) Anal. Biochem. 216:1-14.) Host cell lysis and thermal cycling steps were carried out in a single reaction mixture. Samples were processed and stored in 384-well plates, and the concentration of amplified plasmid DNA was quantified fluorometrically using PICOGREEN dye (Molecular Probes, Inc. (Molecular Probes), Eugene Oreg.) and a FLUOROSKAN II fluorescence scanner (Labsystems Oy, Helsinki, Finland).

[0227] III. Sequencing and Analysis

[0228] cDNA sequencing reactions were processed using standard methods or high-throughput instrumentation such as the ABI CATALYST 800 thermal cycler (Applied Biosystems) or the PTC-200 thermal cycler (MJ Research) in conjunction with the HYDRA microdispenser (Robbins Scientific Corp., Sunnyvale Calif.) or the MICROLAB 2200 liquid transfer system (Hamilton). cDNA sequencing reactions were prepared using reagents provided by Amersham Pharmacia Biotech or supplied in ABI sequencing kits such as the ABI PRISM BIGDYE Terminator cycle sequencing ready reaction kit (Applied Biosystems). Electrophoretic separation of cDNA sequencing reactions and detection of labeled polynucleotides were carried out using the MEGABACE 1000 DNA sequencing system (Molecular Dynamics); the ABI PRISM 373 or 377 sequencing system (Applied Biosystems) in conjunction with standard ABI protocols and base calling software; or other sequence analysis systems known in the art. Reading frames within the cDNA sequences were identified using standard methods (reviewed in Ausubel, 1997, supra, Chapter 7.7). Some of the cDNA sequences were selected for extension using the techniques disclosed in Example VIII.

[0229] IV. Assembly and Analysis of Sequences

[0230] Component sequences from chromatograms were subject to PHRED analysis and assigned a quality score. The sequences having at least a required quality score were subject to various pre-processing editing pathways to eliminate, e.g., low quality 3′ ends, vector and linker sequences, polyA tails, Alu repeats, mitochondrial and ribosomal sequences, bacterial contamination sequences, and sequences smaller than 50 base pairs. In particular, low-information sequences and repetitive elements (e.g., dinucleotide repeats, Alu repeats, etc.) were replaced by “n's”, or masked, to prevent spurious matches.

[0231] Processed sequences were then subject to assembly procedures in which the sequences were assigned to gene bins (bins). Each sequence could only belong to one bin. Sequences in each gene bin were assembled to produce consensus sequences (templates). Subsequent new sequences were added to existing bins using BLASTn (v. 1.4 WashU) and CROSSMATCH. Candidate pairs were identified as all BLAST hits having a quality score greater than or equal to 150. Alignments of at least 82% local identity were accepted into the bin. The component sequences from each bin were assembled using a version of PHRAP. Bins with several overlapping component sequences were assembled using DEEP PHRAP. The orientation (sense or antisense) of each assembled template was determined based on the number and orientation of its component sequences. Template sequences as disclosed in the sequence listing correspond to sense strand sequences (the “forward” reading frames), to the best determination. The complementary (antisense) strands are inherently disclosed herein. The component sequences which were used to assemble each template consensus sequence are listed in Table 5, along with their positions along the template nucleotide sequences.

[0232] Bins were compared against each other and those having local similarity of at least 82% were combined and reassembled. Reassembled bins having templates of insufficient overlap (less than 95% local identity) were re-split. Assembled templates were also subject to analysis by STITCHER/EXON MAPPER algorithms which analyze the probabilities of the presence of splice variants, alternatively spliced exons, splice junctions, differential expression of alternative spliced genes across tissue types or disease states, etc. These resulting bins were subject to several rounds of the above assembly procedures.

[0233] Once gene bins were generated based upon sequence alignments, bins were clone joined based upon clone information. If the 5′sequence of one clone was present in one bin and the 3′ sequence from the same clone was present in a different bin, it was likely that the two bins actually belonged together in a single bin. The resulting combined bins underwent assembly procedures to regenerate the consensus sequences.

[0234] The final assembled templates were subsequently annotated using the following procedure. Template sequences were analyzed using BLASTn (v2.0, NCBI) versus gbpri (GenBank version 124). “Hits” were defined as an exact match having from 95% local identity over 200 base pairs through 100% local identity over 100 base pairs, or a homolog match having an E-value, i.e. a probability score, of <1×10⁻⁸. The hits were subject to frameshift FASTx versus GENPEPT (GenBank version 124). (See Table 8). In this analysis, a homolog match was defined as having an E-value of <1×10⁻⁸. The assembly method used above was described in “System and Methods for Analyzing Biomolecular Sequences,” U.S. Ser. No. 09/276,534, filed Mar. 25, 1999, and the LIFESEQ Gold user manual (Incyte) both incorporated by reference herein.

[0235] Following assembly, template sequences were subjected to motif, BLAST, and functional analyses, and categorized in protein hierarchies using methods described in, e.g., “Database System Employing Protein Function Hierarchies for Viewing Biomolecular Sequence Data,” U.S. Ser. No. 08/812,290, filed Mar. 6, 1997; “Relational Database for Storing Biomolecule Information,” U.S. Ser. No. 08/947,845, filed Oct. 9, 1997; “Project-Based Full-Length Biomolecular Sequence Database,” U.S. Ser. No. 08/811,758, filed Mar. 6, 1997; and “Relational Database and System for Storing Information Relating to Biomolecular Sequences,” U.S. Ser. No. 09/034,807, filed Mar. 4, 1998, all of which are incorporated by reference herein.

[0236] The template sequences were further analyzed by translating each template in all three forward reading frames and searching each translation against the Pfam database of hidden Markov model-based protein families and domains using the HMMER software package (available to the public from Washington University School of Medicine, St. Louis Mo.). Regions of templates which, when translated, contained polarity to Pfam consensus sequences are reported in Table 3, along with descriptions of Pfam protein domains and families. Only those Pfam hits with an E-value of <1×10⁻³ are reported. (See also World Wide Web site http://pfam.wustl.edu/ for detailed descriptions of Pfam protein domains and families.)

[0237] Additionally, the template sequences were translated in all three forward reading frames, and each translation was searched against hidden Markov models for signal peptides using the HMMER software package. Construction of hidden Markov models and their usage in sequence analysis has been described. (See, for example, Eddy, S. R. (1996) Curr. Opin. Str. Biol. 6:361-365.) Only those signal peptide hits with a cutoff score of 11 bits or greater are reported. A cutoff score of 11 bits or greater corresponds to at least about 91-94% true-positives in signal peptide prediction. Template sequences were also translated in all three forward reading frames, and each translation was searched against TMAP, a program that uses weight matrices to delineate transmembrane segments on protein sequences and determine orientation, with respect to the cell cytosol (Persson, B. and P. Argos (1994) J. Mol. Biol. 237:182-192; Persson, B. and P. Argos (1996) Protein Sci. 5:363-371.) Regions of templates which, when translated, contain similarity to signal peptide or transmembrane consensus sequences are reported in Table 4.

[0238] The results of HMMER analysis as reported in Tables 3 and 4 may support the results of BLAST analysis as reported in Table 2 or may suggest alternative or additional properties of template-encoded polypeptides not previously uncovered by BLAST or other analyses.

[0239] Template sequences are further analyzed using the bioinformatics tools listed in Table 8, or using sequence analysis software known in the art such as MACDNASIS PRO software (Hitachi Software Engineering, South San Francisco Calif.) and LASERGENE software (DNASTAR). Template sequences may be further queried against public databases such as the GenBank rodent, mammalian, vertebrate, prokaryote, and eukaryote databases.

[0240] The template sequences were translated to derive the corresponding longest open reading frame as presented by the polypeptide sequences as reported in Table 2. Alternatively, a polypeptide of the invention may begin at any of the methionine residues within the full length translated polypeptide. Polypeptide sequences were subsequently analyzed by querying against the GenBank protein database (GENPEPT, (GenBank version 124)). Full length polynucleotide sequences are also analyzed using MACDNASIS PRO software (Hitachi Software Engineering, South San Francisco Calif.) and LASERGENE software (DNASTAR). Polynucleotide and polypeptide sequence alignments are generated using default parameters specified by the CLUSTAL algorithm as incorporated into the MEGALIGN multisequence alignment program (DNASTAR), which also calculates the percent identity between aligned sequences.

[0241] Table 7 shows sequences with homology to the polypeptides of the invention as identified by BLAST analysis against a GenBank protein (GENPEPT) database. Column 1 shows the polypeptide sequence identification number (SEQ ID NO:) for the polypeptide segments of the invention. Column 2 shows the reading frame used in the translation of the polynucleotide sequences encoding the polypeptide segments. Column 3 shows the length of the translated polypeptide segments. Columns 4 and 5 show the start and stop nucleotide positions of the polynucleotide sequences encoding the polypeptide segments. Column 6 shows the GenBank identification number (GI Number) of the nearest GenBank homolog. Column 7 shows the probability score for the match between each polypeptide and its GenBank homolog. Column 8 shows the annotation of the GenBank homolog.

[0242] V. Analysis of Polynucleotide Expression

[0243] Northern analysis is a laboratory technique used to detect the presence of a transcript of a gene and involves the hybridization of a labeled nucleotide sequence to a membrane on which RNAs from a particular cell type or tissue have been bound. (See, e.g., Sambrook, supra, ch. 7; Ausubel, 1995, supra, ch. 4 and 16.)

[0244] Analogous computer techniques applying BLAST were used to search for identical or related molecules in cDNA databases such as GenBank or LIFESEQ (Incyte Genomics). This analysis is much faster than multiple membrane-based hybridizations. In addition, the sensitivity of the computer search can be modified to determine whether any particular match is categorized as exact or similar. The basis of the search is the product score, which is defined as: $\frac{{BLAST}\quad {Score} \times {Percent}\quad {Identity}}{5 \times {minimum}\quad \left\{ {{{length}\left( {{Seq}.\quad 1} \right)},{{length}\left( {{Seq}.\quad 2} \right)}} \right\}}$

[0245] The product score takes into account both the degree of similarity between two sequences and the length of the sequence match. The product score is a normalized value between 0 and 100, and is calculated as follows: the BLAST score is multiplied by the percent nucleotide identity and the product is divided by (5 times the length of the shorter of the two sequences). The BLAST score is calculated by assigning a score of +5 for every base that matches in a high-scoring segment pair (HSP), and −4 for every mismatch. Two sequences may share more than one HSP (separated by gaps). If there is more than one HSP, then the pair with the highest BLAST score is used to calculate the product score. The product score represents a balance between fractional overlap and quality in a BLAST alignment. For example, a product score of 100 is produced only for 100% identity over the entire length of the shorter of the two sequences being compared. A product score of 70 is produced either by 100% identity and 70% overlap at one end, or by 88% identity and 100% overlap at the other. A product score

is produced either by 100% identity and 50% overlap at one end, or 79% identity and 100% overlap.

[0246] VI. Tissue Distribution Profiling

[0247] A tissue distribution profile is determined for each template by compiling the cDNA library tissue classifications of its component cDNA sequences. Each component sequence, is derived from a cDNA library constructed from a human tissue. Each human tissue is classified into one of the following categories: cardiovascular system; connective tissue; digestive system; embryonic structures; endocrine system; exocrine glands; genitalia, female; genitalia, male; germ cells; hemic and immune system; liver; musculoskeletal system; nervous system; pancreas; respiratory system; sense organs; skin; stomatognathic system; unclassified/mixed; or urinary tract. Template sequences, component sequences, and cDNA library/tissue information are found in the LIFESEQ GOLD database (Incyte Genomics, Palo Alto Calif.).

[0248] Table 6 shows the tissue distribution profile for the templates of the invention. For each template, the three most frequently observed tissue categories are shown in column 3, along with the percentage of component sequences belonging to each category. Only tissue categories with percentage values of ≧10% are shown. A tissue distribution of “widely distributed” in column 3 indicates percentage values of <10% in all tissue categories.

[0249] VII. Transcript Image Analysis

[0250] Transcript images are generated as described in Seilhamer et al., “Comparative Gene Transcript Analysis,” U.S. Pat. No. 5,840,484, incorporated herein by reference.

[0251] VIII. Extension of Polynucleotide Sequences and Isolation of a Full-Length cDNA

[0252] Oligonucleotide primers designed using an mddt of the Sequence Listing are used to extend the nucleic acid sequence. One primer is synthesized to initiate 5′ extension of the template, and the other primer, to initiate 3′ extension of the template. The initial primers may be designed using OLIGO 4.06 software (National Biosciences, Inc. (National Biosciences), Plymouth Minn.), or another appropriate program, to be about 22 to 30 nucleotides in length, to have a GC content of about 50% or more, and to anneal to the target sequence at temperatures of about 68° C. to about 72° C. Any stretch of nucleotides which would result in hairpin structures and primer-primer dimerizations are avoided. Selected human cDNA libraries are used to extend the sequence. If more than one extension is necessary or desired, additional or nested sets of primers are designed.

[0253] High fidelity amplification is obtained by PCR using methods well known in the art. PCR is performed in 96-well plates using the PTC-200 thermal cycler (MJ Research). The reaction mix contains DNA template,

nmol of each primer, reaction buffer containing Mg²⁺, (NH₄)₂SO₄, and β-mercaptoethanol, Taq DNA polymerase (Amersham Pharmacia Biotech), ELONGASE enzyme (Life Technologies), and Pfu DNA polymerase (Stratagene), with the following parameters for primer pair PCI A and PCI B: Step 1: 94° C., 3 min; Step 2: 94° C. 15 sec; Step 3: 60° C., 1 min: Step 4: 68° C. 2 min; Step 5: Steps 2, 3, and 4 repeated 20 times; Step 6: 68° C., 5 min; Step 7: storage at 4° C. In the alternative, the parameters for primer pair T7 and SK+ are as follows: Step 1: 94° C. 3 min; Step 2: 94° C., 15 sec; Step 3: 57° C., 1 min; Step 4: 68° C., 2 min; Step 5: Steps 2, 3, and 4 repeated 20 times; Step 6: 68° C., 5 min; Step 7: storage at 4° C.

[0254] The concentration of DNA in each well is determined by dispensing 100 μl PICOGREEN quantitation reagent (0.25% (v/v); Molecular Probes) dissolved in 1× Tris-EDTA (TE) and 0.5 μl of undiluted PCR product into each well of an opaque fluorimeter plate (Corning Incorporated (Corning), Corning N.Y.), allowing the DNA to bind to the reagent. The plate is scanned in a FLUOROSKAN II (Labsystems Oy) to measure the fluorescence of the sample and to quantify the concentration of DNA. A 5 μl to 10 μl aliquot of the reaction mixture is analyzed by electrophoresis on a 1% agarose mini-gel to determine which reactions are successful in extending the sequence.

[0255] The extended nucleotides are desalted and concentrated, transferred to 384-well plates, digested with CviJI cholera virus endonuclease (Molecular Biology Research, Madison Wis.), and sonicated or sheared prior to religation into pUC 18 vector (Amersham Pharmacia Biotech). For shotgun sequencing, the digested nucleotides are separated on low concentration (0.6 to 0.8%) agarose gels, fragments are excised, and agar digested with AGAR ACE (Promega). Extended clones are religated using T4 ligase (New England Biolabs, Inc., Beverly Mass.) into pUC 18 vector (Amersham Pharmacia Biotech), treated with Pfu DNA polymerase (Stratagene) to fill-in restriction site overhangs, and transfected into competent E. coli cells. Transformed cells are selected on antibiotic-containing media, individual colonies are picked and cultured overnight at 37° C. in 384-well plates in LB/2× carbenicillin liquid media.

[0256] The cells are lysed, and DNA is amplified by PCR using Taq DNA polymerase (Amersham Pharmacia Biotech) and Pfu DNA polymerase (Stratagene) with the following parameters: Step 1: 94° C., 3 min; Step 2: 94° C., 15 sec; Step 3: 60° C., 1 min; Step 4: 72° C., 2 min; Step 5: steps 2, 3, and 4 repeated 29 times; Step 6: 72° C., 5 min; Step 7: storage at 4° C. DNA is quantified by PICOGREEN reagent (Molecular Probes) as described above. Samples with low DNA recoveries are reamplified using the same conditions as described above. Samples are diluted with 20% dimethysulfoxide (1:2, v/v), and sequenced using DYENAMIC energy transfer sequencing primers and the DYENAMIC DIRECT kit (Amersham Pharmacia Biotech) or the ABI PRISM BIGDYE Terminator cycle sequencing ready reaction kit (Applied Biosystems).

[0257] In like manner, the mddt is used to obtain regulatory sequences (promoters, introns, and enhancers) using the procedure above, oligonucleotides designed for su

extension, and an appropriate genomic library.

[0258] IX. Labeling of Probes and Southern Hybridization Analyses

[0259] Hybridization probes derived from the mddt of the Sequence Listing are employed for screening cDNAs, mRNAs, or genomic DNA. The labeling of probe nucleotides between 100 and 1000 nucleotides in length is specifically described, but essentially the same procedure may be used with larger cDNA fragments. Probe sequences are labeled at room temperature for 30 minutes using a T4 polynucleotide kinase, γ³²P-ATP, and 0.5×One-Phor-AII Plus (Amersham Pharmacia Biotech) buffer and purified using a ProbeQuant G-50 Microcolumn (Amersham Pharmacia Biotech). The probe mixture is diluted to 10⁷ dpm/μg/ml hybridization buffer and used in a typical membrane-based hybridization analysis.

[0260] The DNA is digested with a restriction endonuclease such as Eco RV and is electrophoresed through a 0.7% agarose gel. The DNA fragments are transferred from the agarose to nylon membrane (NYTRAN Plus, Schleicher & Schuell, Inc., Keene N.H.) using procedures specified by the manufacturer of the membrane. Prehybridization is carried out for three or more hours at 68° C., and hybridization is carried out overnight at 68° C. To remove non-specific signals, blots are sequentially washed at room temperature under increasingly stringent conditions, up to 0.1× saline sodium citrate (SSC) and 0.5% sodium dodecyl sulfate. After the blots are placed in a PHOSPHORIMAGER cassette (Molecular Dynamics) or are exposed to autoradiography film, hybridization patterns of standard and experimental lanes are compared. Essentially the same procedure is employed when screening RNA.

[0261] X. Chromosome Mapping of mddt

[0262] The cDNA sequences which were used to assemble SEQ ID NO:1-252 are compared with sequences from the Incyte LIFESEQ database and public domain databases using BLAST and other implementations of the Smith-Waterman algorithm. Sequences from these databases that match SEQ ID NO:1-252 are assembled into clusters of contiguous and overlapping sequences using assembly algorithms such as PHRAP (Table 8). Radiation hybrid and genetic mapping data available from public resources such as the Stanford Human Genome Center (SHGC), Whitehead Institute for Genome Research (WIGR), and Généthon are used to determine if any of the clustered sequences have been previously mapped. Inclusion of a mapped sequence in a cluster will result in the assignment of all sequences of that cluster, including its particular SEQ ID NO:, to that map location. The genetic map locations of SEQ ID NO:1-252 are described as ranges, or intervals, of human chromosomes. The map position of an interval, in centiMorgans, is measured relative to the terminus of the chromosome's p-

. The centiMorgan (cM) is a unit of measurement based on recombination frequencies between chromosomal markers. On average, 1 cM is roughly equivalent to 1 megabase (Mb) of DNA in humans, although this can vary widely due to hot and cold spots of recombination.) The cM distances are based on genetic markers mapped by Généthon which provide boundaries for radiation hybrid markers whose sequences were included in each of the clusters.

[0263] XI. Microarray Analysis

[0264] Probe Preparation from Tissue or Cell Samples

[0265] Total RNA is isolated from tissue samples using the guanidinium thiocyanate method and polyA⁺ RNA is purified using the oligo (dT) cellulose method. Each polyA⁺ RNA sample is reverse transcribed using MMLV reverse-transcriptase, 0.05 pg/μl oligo-dT primer (21mer), 1× first strand buffer, 0.03 units/μl RNase inhibitor, 500 μM dATP, 500 μM dGTP, 500 μM dTTP, 40 μM dCTP, 40 μM dCTP-Cy3 (BDS) or dCTP-Cy5 (Amersham Pharmacia Biotech). The reverse transcription reaction is performed in a 25 ml volume containing 200 ng polyA⁺ RNA with GEMBRIGHT kits (Incyte). Specific control polyA⁺ RNAs are synthesized by in vitro transcription from non-coding yeast genomic DNA (W. Lei, unpublished). As quantitative controls, the control mRNAs at 0.002 ng, 0.02 ng, 0.2 ng, and 2 ng are diluted into reverse transcription reaction at ratios of 1:100,000, 1:10,000, 1:1000, 1:100 (w/w) to sample mRNA respectively. The control mRNAs are diluted into reverse transcription reaction at ratios of 1:3, 3:1, 1:10, 10:1, 1:25, 25:1 (w/w) to sample mRNA differential expression patterns. After incubation at 37° C. for 2 hr, each reaction sample (one with Cy3 and another with Cy5 labeling) is treated with 2.5 ml of 0.5M sodium hydroxide and incubated for 20 minutes at 85° C. to the stop the reaction and degrade the RNA. Probes are purified using two successive CHROMA SPIN 30 gel filtration spin columns (CLONTECH Laboratories, Inc. (CLONTECH), Palo Alto Calif.) and after combining, both reaction samples are ethanol precipitated using 1 ml of glycogen (1 mg/ml), 60 ml sodium acetate, and 300 ml of 100% ethanol. The probe is then dried to completion using a SpeedVAC (Savant Instruments Inc., Holbrook N.Y.) and resuspended in 14 μl 5×SSC/0.2% SDS.

[0266] Microarray Preparation

[0267] Sequences of the present invention are used to generate array elements. Each array element is amplified from bacterial cells containing vectors with cloned cDNA inserts. PCR amplification uses primers complementary to the vector sequences flanking the cDNA insert. Array elements are amplified in thirty cycles of PCR from an initial quantity of 1-2 ng to a final quantity greater than 5 μg. Amplified array elements are then purified using SEPHACRYL-400 (Amersham Pharmacia Biotech).

[0268] Purified array elements are immobilized on polymer-coated glass slides. Glass microscope slides (Corning) are cleaned by ultrasound in 0.1% SDS and acetone, with extensive distilled water washes between and after treatments. Glass slides are etched in 4% hydrofluoric acid (VWR Scientific Products Corporation (VWR), West Chester, Pa.), washed extensively in distilled water, and coated with 0.05% aminopropyl silane (Sigma) in 95% ethanol. Coated slides are cured in a 110° C. oven.

[0269] Array elements are applied to the coated glass substrate using a procedure described in U.S. Pat. No. 5,807,522, incorporated herein by reference. 1 μl of the array element DNA, at an average concentration of 100 ng/μl, is loaded into the open capillary printing element by a high-speed robotic apparatus. The apparatus then deposits about 5 nl of array element sample per slide.

[0270] Microarrays are UV-crosslinked using a STRATALINKER UV-crosslinker (Stratagene). Microarrays are washed at room temperature once in 0.2% SDS and three times in distilled water. Non-specific binding sites are blocked by incubation of microarrays in 0.2% casein in phosphate buffered saline (PBS) (Tropix, Inc., Bedford, Mass.) for 30 minutes at 60° C. followed by washes in 0.2% SDS and distilled water as before.

[0271] Hybridization

[0272] Hybridization reactions contain 9 μl of probe mixture consisting of 0.2 μg each of Cy3 and Cy5 labeled cDNA synthesis products in 5×SSC, 0.2% SDS hybridization buffer. The probe mixture is heated to 65° C. for 5 minutes and is aliquoted onto the microarray surface and covered with an 1.8 cm² coverslip. The arrays are transferred to a waterproof chamber having a cavity just slightly larger than a microscope slide. The chamber is kept at 100% humidity internally by the addition of 140 μl of 5×SSC in a corner of the chamber. The chamber containing the arrays is incubated for about 6.5 hours at 60° C. The arrays are washed for 10 min at 45° C. in a first wash buffer (1×SSC, 0.1% SDS), three times for 10 minutes each at 45° C. in a second wash buffer (0.1×SSC), and dried.

[0273] Detection

[0274] Reporter-labeled hybridization complexes are detected with a microscope equipped with an Innova 70 mixed gas 10 W laser (Coherent, Inc., Santa Clara Calif.) capable of generating spectral lines at 488 nm for excitation of Cy3 and at 632 nm for excitation of Cy5. The excitation laser light is focused on the array using a 20× microscope objective (Nikon, Inc., Melville N.Y.). The slide containing the array is placed on a computer-controlled X-Y stage on the microscope and raster-scanned past the objective. The 1.8 cm×1.8 cm array used in the present example is scanned with a resolution of 20 micrometers.

[0275] In two separate scans, a mixed gas multiline laser excites the two fluorophores sequentially. Emitted light is split, based on wavelength, into two photomultiplier tube detectors (PMT R1477, Hamamatsu Photonics Systems, Bridgewater N.J.) corresponding to the two fluorophores. Appropriate filters positioned between the array and the photomultiplier tubes are used to filter the signals. The emission maxima of the fluorophores used are 565 nm for Cy3 and 650 nm for Cy5. Each array is typically scanned twice, one scan per fluorophore using the appropriate filters at the laser source, although the apparatus is capable of recording the spectra from both fluorophores simultaneously.

[0276] The sensitivity of the scans is typically calibrated using the signal intensity generated by a cDNA control species added to the probe mix at a known concentration. A specific location on the array contains a complementary DNA sequence, allowing the intensity of the signal at that location to be correlated with a weight ratio of hybridizing species of 1:100,000. When two probes from different sources (e.g., representing test and control cells), each labeled with a different fluorophore, are hybridized to a single array for the purpose of identifying genes that are differentially expressed, the calibration is done by labeling samples of the calibrating cDNA with the two fluorophores and adding identical amounts of each to the hybridization mixture.

[0277] The output of the photomultiplier tube is digitized using a 12-bit RTI-835H analog-to-digital (A/D) conversion board (Analog Devices, Inc., Norwood, Mass.) installed in an IBM-compatible PC computer. The digitized data are displayed as an image where the signal intensity is mapped using a linear 20-color transformation to a pseudocolor scale ranging from blue (low signal) to red (high signal). The data is also analyzed quantitatively. Where two different fluorophores are excited and measured simultaneously, the data are first corrected for optical crosstalk (due to overlapping emission spectra) between the fluorophores using each fluorophore's emission spectrum.

[0278] A grid is superimposed over the fluorescence signal image such that the signal from each spot is centered in each element of the grid. The fluorescence signal within each element is then integrated to obtain a numerical value corresponding to the average intensity of the signal. The software used for signal analysis is the GEMTOOLS gene expression analysis program (Incyte).

[0279] XII. Complementary Nucleic Acids

[0280] Sequences complementary to the mddt are used to detect, decrease, or inhibit expression of the naturally occurring nucleotide. The use of oligonucleotides comprising from about 15 to 30 base pairs is typical in the art. However, smaller or larger sequence fragments can also be used. Appropriate oligonucleotides are designed from the mddt using OLIGO 4.06 software (National Biosciences) or other appropriate programs and are synthesized using methods standard in the art or ordered from a commercial supplier. To inhibit transcription, a complementary oligonucleotide is designed from the most unique 5′ sequence and used to prevent transcription factor binding to the promoter sequence. To inhibit translation, a complementary oligonucleotide is designed to prevent ribosomal binding and processing of the transcript.

[0281] XIII. Expression of MDDT

[0282] Expression and purification of MDDT is accomplished using bacterial or virus-based expression systems. For expression of MDDT in bacteria, cDNA is subcloned into an appropriate vector containing an antibiotic resistance gene and an inducible promoter that directs high levels of cDNA transcription. Examples of such promoters include, but are not limited to, the trp-lac (tac) hybrid promoter and the T5 or T7 bacteriophage promoter in conjunction with the lac operator regulatory element. Recombinant vectors are transformed into suitable bacterial hosts. e.g., BL21(DE3). Antibiotic resistant bacteria express MDDT upon induction with isopropyl beta-D-thiogalactopyranoside (IPTG). Expression of MDDT in eukaryotic cells is achieved by infecting insect or mammalian cell lines with recombinant Autographica californica nuclear polyhedrosis virus (AcMNPV), commonly known as baculovirus. The nonessential polyhedrin gene of baculovirus is replaced with cDNA encoding MDDT by either homologous recombination or bacterial-mediated transposition involving transfer plasmid intermediates. Viral infectivity is maintained and the strong polyhedrin promoter drives high levels of cDNA transcription. Recombinant baculovirus is used to infect Spodoptera frugiperda (Sf9) insect cells in most cases, or human hepatocytes, in some cases. Infection of the latter requires additional genetic modifications to baculovirus. (See e.g., Engelhard, supra, and Sandig, supra.)

[0283] In most expression systems, MDDT is synthesized as a fusion protein with, e.g., glutathione S-transferase (GST) or a peptide epitope tag, such as FLAG or 6-His, permitting rapid, single-step, affinity-based purification of recombinant fusion protein from crude cell lysates. GST, a 26-kilodalton enzyme from Schistosoma japonicum, enables the purification of fusion proteins on immobilized glutathione under conditions that maintain protein activity and antigenicity (Amersham Pharmacia Biotech). Following purification, the GST moiety can be proteolytically cleaved from MDDT at specifically engineered sites. FLAG, an 8-amino acid peptide, enables immunoaffinity purification using commercially available monoclonal and polyclonal anti-FLAG antibodies (Eastman Kodak Company, Rochester N.Y.). 6-His, a stretch of six consecutive histidine residues, enables purification on metal-chelate resins (QIAGEN). Methods for protein expression and purification are discussed in Ausubel (1995, supra, Chapters 10 and 16). Purified MDDT obtained by these methods can be used directly in the following activity assay.

[0284] XIV. Demonstration of MDDT Activity

[0285] MDDT, or biologically active fragments thereof, are labeled with ²⁵¹I Bolton-Hunter reagent. (See, e.g., Bolton, A. E. and W. M. Hunter (1973) Biochem. J. 133:529-539.) Candidate molecules previously arrayed in the wells of a multi-well plate are incubated with the labeled MDDT, washed, and any wells with labeled MDDT complex are assayed. Data obtained using different concentrations of MDDT are used to calculate values for the number, affinity, and association of MDDT with the candidate molecules.

[0286] Alternatively, molecules interacting with MDDT are analyzed using the yeast two-hybrid system as described in Fields, S. and O. Song (1989) Nature 340:245-246, or using commercially available kits based on the two-hybrid system, such as the MATCHMAKER system (CLONTECH).

[0287] MDDT may also be used in the PATHCALLING process (CuraGen Corp. New Haven Conn.) which employs the yeast two-hybrid system in a high-throughput manner to determine all interactions between the proteins encoded by two large libraries of genes (Nandabalan, K. et al. (2000) U.S. Pat. No. 6,057,101).

[0288] XV. Functional Assays

[0289] MDDT function is assessed by expressing mddt at physiologically elevated levels in mammalian cell culture systems. cDNA is subcloned into a mammalian expression vector containing a strong promoter that drives high levels of cDNA expression. Vectors of choice include pCMV SPORT (Life Technologies) and pCR3.1 (Invitrogen Corporation, Carlsbad Calif.), both of which contain the cytomegalovirus promoter. 5-10 μg of recombinant vector are transiently transfected into a human cell line, preferably of endothelial or hematopoietic origin, using either liposome formulations or electroporation. 1-2 μg of an additional plasmid containing sequences encoding a marker protein are co-transfected.

[0290] Expression of a marker protein provides a means to distinguish transfected cells from nontransfected cells and is a reliable predictor of cDNA expression from the recombinant vector. Marker proteins of choice include, e.g., Green Fluorescent Protein (GFP; CLONTECH), CD64, or a CD64-GFP fusion protein. Flow cytometry (FCM), an automated laser optics-based technique, is used to identify transfected cells expressing GFP or CD64-GFP and to evaluate the apoptotic state of the cells and other cellular properties.

[0291] FCM detects and quantifies the uptake of fluorescent molecules that diagnose events preceding or coincident with cell death. These events include changes in nuclear DNA content as measured by staining of DNA with propidium iodide; changes in cell size and granularity as measured by forward light scatter and 90 degree side light scatter; down-regulation of DNA synthesis as measured by decrease in bromodeoxyuridine uptake; alterations in expression of cell surface and intracellular proteins as measured by reactivity with specific antibodies; and alterations in plasma membrane composition as measured by the binding of fluorescein-conjugated Annexin V protein to the cell surface. Methods in flow cytometry are discussed in Ormerod, M. G. (1994) Flow Cytometry, Oxford, New York N.Y.

[0292] The influence of MDDT on gene expression can be assessed using highly purified populations of cells transfected with sequences encoding MDDT and either CD64 or CD64-GFP. CD64 and CD64-GFP are expressed as the surface of transfected cells and bind to observed regions of human immunoglobulin G (IgG). Transfected cells are efficiently separated from nontransfected cells using magnetic beads coated with either human IgG or antibody against CD64 (DYNAL, Inc., Lake Success N.Y.). mRNA can be purified from the cells using methods well known by those of skill in the art. Expression of mRNA encoding MDDT and other genes of interest can be analyzed by northern analysis or microarray techniques.

[0293] XVI. Production of Antibodies

[0294] MDDT substantially purified using polyacrylamide gel electrophoresis (PAGE; see, e.g., Harrington, M. G. (1990) Methods Enzymol. 182:488-495), or other purification techniques, is used to immunize rabbits and to produce antibodies using standard protocols.

[0295] Alternatively, the MDDT amino acid sequence is analyzed using LASERGENE software (DNASTAR) to determine regions of high immunogenicity, and a corresponding peptide is synthesized and used to raise antibodies by means known to those of skill in the art. Methods for selection of appropriate epitopes, such as those near the C-terminus or in hydrophilic regions are well described in the art. (See, e.g., Ausubel, 1995, supra, Chapter 11.)

[0296] Typically, peptides 15 residues in length are synthesized using an ABI 431A peptide synthesizer (Applied Biosystems) using fmoc-chemistry and coupled to KLH (Sigma) by reaction with N-maleimidobenzoyl-N-hydroxysuccinimide ester (MBS) to increase immunogenicity. (See, e.g., Ausubel, supra.) Rabbits are immunized with the peptide-KLH complex in complete Freund's adjuvant. Resulting antisera are tested for antipeptide activity by, for example, binding the peptide to plastic, blocking with 1% BSA, reacting with rabbit antisera, washing, and reacting with radio-iodinated goat anti-rabbit IgG. Antisera with antipeptide activity are tested for anti-MDDT activity using protocols well known in the art, including ELISA, RIA, and immunoblotting.

[0297] XVII. Purification of Naturally Occurring MDDT Using Specific Antibodies

[0298] Naturally occurring or recombinant MDDT is substantially purified by immunoaffinity chromatography using antibodies specific for MDDT. An immunoaffinity column is constructed by covalently coupling anti-MDDT antibody to an activated chromatographic resin, such as CNBr-activated SEPHAROSE (Amersham Pharmacia Biotech). After the coupling, the resin is blocked and washed according to the manufacturer's instructions.

[0299] Media containing MDDT are passed over the immunoaffinity column, and the column is washed under conditions that allow the preferential absorbance of MDDT (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/MDDT binding (e.g., a buffer of pH 2 to pH 3, or a high concentration of a chaotrope, such as urea or thiocyanate io

nd MDDT is collected.

[0300] All publications and patents mentioned in the above specification are herein incorporated by reference. Various modifications and variations of the described method and system of the invention will be apparent to those skilled in the art without departing from the scope and spirit of the invention. Although the invention has been described in connection with specific preferred embodiments, it should be understood that the invention as claimed should not be unduly limited to such specific embodiments. Indeed, various modifications of the above-described modes for carrying out the invention which are obvious to those skilled in the field of molecular biology or related fields are intended to be within the scope of the following claims. TABLE 1 SEQ ID NO: Template ID SEQ ID NO: ORF ID 1 LG:150318.1:2000SEP08 253 LG:150318.1.orf2:2000SEP08 2 LG:022529.1:2000SEP08 254 LG:022529.1.orf1:2000SEP08 3 LG:352559.1:2000SEP08 255 LG:352559.1.orf2:2000SEP08 4 LG:175223.1:2000SEP08 256 LG:175223.1.orf3:2000SEP08 5 LG:476989.1:2000SEP08 257 LG:476989.1.orf2:2000SEP08 6 LG:253268.7:2000SEP08 258 LG:253268.7.orf1:2000SEP08 7 LG:401322.1:2000SEP08 259 LG:401322.1.orf1:2000SEP08 8 LG:1328436.1:2000SEP08 260 LG:1328436.1.orf2:2000SEP08 9 LG:475404.1:2000SEP08 261 LG:475404.1.orf2:2000SEP08 10 LG:1384132.1:2000SEP08 262 LG:1384132.1.orf1:2000SEP08 11 LG:410804.18:2000SEP08 263 LG:410804.18.orf1:2000SEP08 12 LG:1082306.1:2000SEP08 264 LG:1082306.1.orf1:2000SEP08 13 LG:233814.4:2000SEP08 265 LG:233814.4.orf1:2000SEP08 14 LG:977478.5:2000SEP08 266 LG:977478.5.orf3:2000SEP08 15 LG:025931.1:2000SEP08 267 LG:025931.1.orf2:2000SEP08 16 LG:885368.1:2000SEP08 268 LG:885368.1.orf1:2000SEP08 17 LG:1054900.1:2000SEP08 269 LG:1054900.1.orf3:2000SEP08 18 LG:995186.2:2000SEP08 270 LG:995186.2.orf3:2000SEP08 19 LG:435048.23:2000SEP08 271 LG:435048.23.orf2:2000SEP08 20 LG:954859.1:2000SEP08 272 LG:954859.1.orf2:2000SEP08 21 LG:364370.1:2000SEP08 273 LG:364370.1.orf3:2000SEP08 22 LG:1098789.1:2000SEP08 274 LG:1098789.1.orf3:2000SEP08 23 LG:201540.2:2000SEP08 275 LG:201540.2.orf2:2000SEP08 24 LG:1077357.1:2000SEP08 276 LG:1077357.1.orf1:2000SEP08 25 LG:1048846.4:2000SEP08 277 LG:1048846.4.orf3:2000SEP08 26 LG:336685.1:2000SEP08 278 LG:336685.1.orf3:2000SEP08 27 LG:1076253.1:2000SEP08 279 LG:1076253.1.orf3:2000SEP08 28 LG:1400601.2:2000SEP08 280 LG:1400601.2.orf3:2000SEP08 29 LG:1079092.3:2000SEP08 281 LG:1079092.3.orf2:2000SEP08 30 LG:1086064.1:2000SEP08 282 LG:1086064.1.orf2:2000SEP08 31 LG:1400608.1:2000SEP08 283 LG:1400608.1.orf3:2000SEP08 32 LG:399275.5:2000SEP08 284 LG:399275.5.orf1:2000SEP08 33 LG:293943.1:2000SEP08 285 LG:293943.1.orf1:2000SEP08 34 LG:345884.1:2000SEP08 286 LG:345884.1.orf2:2000SEP08 35 LG:400967.1:2000SEP08 287 LG:400967.1.orf1:2000SEP08 36 LG:024556.6:2000SEP08 288 LG:024556.6.orf1:2000SEP08 37 LG:081189.3:2000SEP08 289 LG:081189.3.orf2:2000SEP08 38 LG:018258.1:2000SEP08 290 LG:018258.1.orf3:2000SEP08 39 LG:450399.3:2000SEP08 291 LG:450399.3.orf3:2000SEP08 40 LG:451122.1:2000SEP08 292 LG:451122.1.orf1:2000SEP08 41 LG:451682.1:2000SEP08 293 LG:451682.1.orf3:2000SEP08 42 LG:238631.4:2000SEP08 294 LG:238631.4.orf3:2000SEP08 43 LG:236654.1:2000SEP08 295 LG:236654.1.orf3:2000SEP08 44 LG:332655.1:2000SEP08 296 LG:332655.1.orf1:2000SEP08 45 LG:217396.2:2000SEP08 297 LG:217396.2.orf1:2000SEP08 46 LG:090574.1:2000SEP08 298 LG:090574.1.orf3:2000SEP08 47 LG:202943.1:2000SEP08 299 LG:202943.1.orf1:2000SEP08 48 LG:236928.1:2000SEP08 300 LG:236928.1.orf1:2000SEP08 49 LG:215169.2:2000SEP08 301 LG:215169.2.orf2:2000SEP08 50 LG:410726.1:2000SEP08 302 LG:410726.1.orf1:2000SEP08 51 LG:234372.2:2000SEP08 303 LG:234372.2.orf2:2000SEP08 52 LG:022629.1:2000SEP08 304 LG:022629.1.orf3:2000SEP08 53 LG:068682.1:2000SEP08 305 LG:068682.1.orf2:2000SEP08 54 LG:222335.1:2000SEP08 306 LG:222335.1.orf1:2000SEP08 55 LG:331342.1:2000SEP08 307 LG:331342.1.orf3:2000SEP08 56 LG:021770.1:2000SEP08 308 LG:021770.1.orf3:2000SEP08 57 LG:181607.9:2000SEP08 309 LG:181607.9.orf2:2000SEP08 58 LG:1042768.1:2000SEP08 310 LG:1042768.1.orf3:2000SEP08 59 LG:282729.1:2000SEP08 311 LG:282729.1.orf1:2000SEP08 60 LG:998305.3:2000SEP08 312 LG:998305.3.orf2:2000SEP08 61 LG:1135213.1:2000SEP08 313 LG:1135213.1.orf1:2000SEP08 62 LG:267762.1:2000SEP08 314 LG:267762.1.orf1:2000SEP08 63 LG:120744.1:2000SEP08 315 LG:120744.1.orf1:2000SEP08 64 LG:403409.1:2000SEP08 316 LG:403409.1.orf3:2000SEP08 65 LG:226874.3:2000SEP08 317 LG:226874.3.orf1:2000SEP08 66 LG:1045521.4:2000SEP08 318 LG:1045521.4.orf1:2000SEP08 67 LG:275876.1:2000SEP08 319 LG:275876.1.orf1:2000SEP08 68 LG:475127.7:2000SEP08 320 LG:475127.7.orf1:2000SEP08 69 LG:157263.1:2000SEP08 321 LG:157263.1.orf1:2000SEP08 70 LG:247382.7:2000SEP08 322 LG:247382.7.orf1:2000SEP08 71 LG:197367.5:2000SEP08 323 LG:197367.5.orf2:2000SEP08 72 LG:218090.5:2000SEP08 324 LG:218090.5.orf2:2000SEP08 73 LG:216612.4:2000SEP08 325 LG:216612.4.orf3:2000SEP08 74 LG:197614.1:2000SEP08 326 LG:197614.1.orf1:2000SEP08 75 LG:378428.1:2000SEP08 327 LG:378428.1.orf3:2000SEP08 76 LG:286639.1:2000SEP08 328 LG:286639.1.orf3:2000SEP08 77 LG:389870.1:2000SEP08 329 LG:389870.1.orf1:2000SEP08 78 LG:1387485.6:2000SEP08 330 LG:1387485.6.orf2:2000SEP08 79 LG:230151.1:2000SEP08 331 LG:230151.1.orf1:2000SEP08 80 LG:215158.5:2000SEP08 332 LG:215158.5.orf1:2000SEP08 81 LG:235840.1:2000SEP08 333 LG:235840.1.orf2:2000SEP08 82 LG:350272.1:2000SEP08 334 LG:350272.1.orf2:2000SEP08 83 LG:232190.1:2000SEP08 335 LG:232190.1.orf2:2000SEP08 84 LG:1068127.1:2000SEP08 336 LG:1068127.1.orf2:2000SEP08 85 LG:408751.3:2000SEP08 337 LG:408751.3.orf2:2000SEP08 86 LG:1078933.1:2000SEP08 338 LG:1078933.1.orf1:2000SEP08 87 LG:958731.1:2000SEP08 339 LG:958731.1.orf3:2000SEP08 88 LG:024125.5:2000SEP08 340 LG:024125.5.orf3:2000SEP08 89 LG:373637.3:2000SEP08 341 LG:373637.3.orf1:2000SEP08 90 LG:1053229.1:2000SEP08 342 LG:1053229.1.orf1:2000SEP08 91 LG:248364.1:2000SEP08 343 LG:248364.1.orf2:2000SEP08 92 LG:477130.1:2000SEP08 344 LG:477130.1.orf3:2000SEP08 93 LG:113786.17:2000SEP08 345 LG:113786.17.orf2:2000SEP08 94 LG:347635.1:2000SEP08 346 LG:347635.1.orf3:2000SEP08 95 LG:242966.4:2000SEP08 347 LG:242966.4.orf1:2000SEP08 96 LG:217814.1:2000SEP08 348 LG:217814.1.orf3:2000SEP08 97 LG:476452.1:2000SEP08 349 LG:476452.1.orf3:2000SEP08 98 LG:1100657.1:2000SEP08 350 LG:1100657.1.orf1:2000SEP08 99 LG:1132418.2:2000SEP08 351 LG:1132418.2.orf1:2000SEP08 100 LG:1098570.1:2000SEP08 352 LG:1098570.1.orf3:2000SEP08 101 LG:1097987.1:2000SEP08 353 LG:1097987.1.orf3:2000SEP08 102 LG:337818.2:2000SEP08 354 LG:337818.2.orf1:2000SEP08 103 LG:1040582.1:2000SEP08 355 LG:1040582.1.orf2:2000SEP08 104 LG:1099122.1:2000SEP08 356 LG:1099122.1.orf3:2000SEP08 105 LG:1327449.1:2000SEP08 357 LG:1327449.1.orf3:2000SEP08 106 LG:227933.5:2000SEP08 358 LG:227933.5.orf1:2000SEP08 107 LG:1043709.2:2000SEP08 359 LG:1043709.2.orf3:2000SEP08 108 LG:1099871.1:2000SEP08 360 LG:1099871.1.orf1:2000SEP08 109 LG:1399139.4:2000SEP08 361 LG:1399139.4.orf3:2000SEP08 110 LG:236386.1:2000SEP08 362 LG:236386.1.orf3:2000SEP08 111 LG:1015157.1:2000SEP08 363 LG:1015157.1.orf1:2000SEP08 112 LG:1065433.1:2000SEP08 364 LG:1065433.1.orf3:2000SEP08 113 LG:236992.4:2000SEP08 365 LG:236992.4.orf1:2000SEP08 114 LG:1071124.1:2000SEP08 366 LG:1071124.1.orf1:2000SEP08 115 LG:206425.2:2000SEP08 367 LG:206425.2.orf2:2000SEP08 116 LG:885747.2:2000SEP08 368 LG:885747.2.orf3:2000SEP08 117 LG:1140501.1:2000SEP08 369 LG:1140501.1.orf1:2000SEP08 118 LG:001239.1:2000SEP08 370 LG:001239.1.orf3:2000SEP08 119 LG:018980.1:2000SEP08 371 LG:018980.1.orf1:2000SEP08 120 LG:1083120.3:2000SEP08 372 LG:1083120.3.orf3:2000SEP08 121 LG:233258.3:2000SEP08 373 LG:233258.3.orf3:2000SEP08 122 LG:999062.1:2000SEP08 374 LG:999062.1.orf3:2000SEP08 123 LG:887776.1:2000SEP08 375 LG:887776.1.orf3:2000SEP08 124 LG:1400301.2:2000SEP08 376 LG:1400301.2.orf1:2000SEP08 125 LG:1329362.1:2000SEP08 377 LG:1329362.1.orf2:2000SEP08 126 LG:1096498.1:2000SEP08 378 LG:1096498.1.orf2:2000SEP08 127 LG:1096337.1:2000SEP08 379 LG:1096337.1.orf2:2000SEP08 128 LG:1400579.1:2000SEP08 380 LG:1400579.1.orf2:2000SEP08 129 LG:1080091.1:2000SEP08 381 LG:1080091.1.orf2:2000SEP08 129 LG:1080091.1:2000SEP08 382 LG:1080091.1.orf3:2000SEP08 130 LG:1082203.1:2000SEP08 383 LG:1082203.1.orf1:2000SEP08 131 LG:1084051.1:2000SEP08 384 LG:1084051.1.orf3:2000SEP08 132 LG:1082393.1:2000SEP08 385 LG:1082393.1.orf3:2000SEP08 133 LG:1086183.1:2000SEP08 386 LG:1086183.1.orf2:2000SEP08 134 LG:1090268.1:2000SEP08 387 LG:1090268.1.orf3:2000SEP08 135 LG:1400597.5:2000SEP08 388 LG:1400597.5.orf1:2000SEP08 136 LG:1080307.2:2000SEP08 389 LG:1080307.2.orf3:2000SEP08 137 LG:1400603.2:2000SEP08 390 LG:1400603.2.orf2:2000SEP08 138 LG:1052984.1:2000SEP08 391 LG:1052984.1.orf1:2000SEP08 139 LG:1091259.1:2000SEP08 392 LG:1091259.1.orf3:2000SEP08 140 LG:1082263.2:2000SEP08 393 LG:1082263.2.orf3:2000SEP08 141 LG:1048604.2:2000SEP08 394 LG:1048604.2.orf3:2000SEP08 142 LG:1085254.3:2000SEP08 395 LG:1085254.3.orf2:2000SEP08 143 LG:1400606.2:2000SEP08 396 LG:1400606.2.orf1:2000SEP08 144 LG:1090358.2:2000SEP08 397 LG:1090358.2.orf1:2000SEP08 145 LG:1079064.2:2000SEP08 398 LG:1079064.2.orf1:2000SEP08 146 LG:1076866.1:2000SEP08 399 LG:1076866.1.orf2:2000SEP08 147 LG:969359.1:2000SEP08 400 LG:969359.1.orf2:2000SEP08 148 LG:366783.1:2000SEP08 401 LG:366783.1.orf1:2000SEP08 149 LG:332176.3:2000SEP08 402 LG:332176.3.orf2:2000SEP08 150 LG:994938.1:2000SEP08 403 LG:994938.1.orf3:2000SEP08 151 LG:982800.1:2000SEP08 404 LG:982800.1.orf1:2000SEP08 152 LG:977850.7:2000SEP08 405 LG:977850.7.orf1:2000SEP08 153 LG:234748.2:2000SEP08 406 LG:234748.2.orf3:2000SEP08 154 LG:306284.1:2000SEP08 407 LG:306284.1.orf2:2000SEP08 155 LI:333170.3:2000SEP08 408 LI:333170.3.orf1:2000SEP08 156 LI:336685.2:2000SEP08 409 LI:336685.2.orf3:2000SEP08 157 LI:279013.5:2000SEP08 410 LI:279013.5.orf3:2000SEP08 158 LI:1037075.1:2000SEP08 411 LI:1037075.1.orf1:2000SEP08 159 LI:1073403.1:2000SEP08 412 LI:1073403.1.orf2:2000SEP08 160 LI:1075296.1:2000SEP08 413 LI:1075296.1.orf1:2000SEP08 161 LI:1085501.1:2000SEP08 414 LI:1085501.1.orf3:2000SEP08 162 LI:1086181.1:2000SEP08 415 LI:1086181.1.orf2:2000SEP08 163 LI:1164493.1:2000SEP08 416 LI:1164493.1.orf1:2000SEP08 164 LI:1175097.1:2000SEP08 417 LI:1175097.1.orf1:2000SEP08 165 LI:1092948.1:2000SEP08 418 LI:1092948.1.orf2:2000SEP08 166 LI:380378.2:2000SEP08 419 LI:380378.2.orf3:2000SEP08 167 LI:1029674.1:2000SEP08 420 LI:1029674.1.orf3:2000SEP08 168 LI:2048601.3:2000SEP08 421 LI:2048601.3.orf2:2000SEP08 169 LI:1186208.1:2000SEP08 422 LI:1186208.1.orf2:2000SEP08 170 LI:1170753.1:2000SEP08 423 LI:1170753.1.orf1:2000SEP08 171 LI:1180908.1:2000SEP08 424 LI:1180908.1.orf2:2000SEP08 172 LI:1182900.2:2000SEP08 425 LI:1182900.2.orf1:2000SEP08 173 LI:1169548.2:2000SEP08 426 LI:1169548.2.orf3:2000SEP08 174 LI:1039974.1:2000SEP08 427 LI:1039974.1.orf1:2000SEP08 175 LI:1175765.2:2000SEP08 428 LI:1175765.2.orf3:2000SEP08 176 LI:313948.1:2000SEP08 429 LI:313948.1.orf3:2000SEP08 177 LI:335923.2:2000SEP08 430 LI:335923.2.orf2:2000SEP08 178 LI:345884.1:2000SEP08 431 LI:345884.1.orf1:2000SEP08 179 LI:417127.1:2000SEP08 432 LI:417127.1.orf1:2000SEP08 180 LI:451710.1:2000SEP08 433 LI:451710.1.orf1:2000SEP08 181 LI:406882.2:2000SEP08 434 LI:406882.2.orf1:2000SEP08 182 LI:728223.1:2000SEP08 435 LI:728223.1.orf2:2000SEP08 183 LI:289783.19:2000SEP08 436 LI:289783.19.orf2:2000SEP08 184 LI:235255.8:2000SEP08 437 LI:235255.8.orf2:2000SEP08 185 LI:237693.5:2000SEP08 438 LI:237693.5.orf3:2000SEP08 186 LI:433670.3:2000SEP08 439 LI:433670.3.orf2:2000SEP08 187 LI:202943.4:2000SEP08 440 LI:202943.4.orf2:2000SEP08 188 LI:068682.1:2000SEP08 441 LI:068682.1.orf1:2000SEP08 189 LI:203301.3:2000SEP08 442 LI:203301.3.orf2:2000SEP08 190 LI:020726.3:2000SEP08 443 LI:020726.3.orf2:2000SEP08 191 LI:027209.1:2000SEP08 444 LI:027209.1.orf1:2000SEP08 192 LI:108819.1:2000SEP08 445 LI:108819.1.orf1:2000SEP08 193 LI:021759.1:2000SEP08 446 LI:021759.1.orf2:2000SEP08 194 LI:1165967.1:2000SEP08 447 LI:1165967.1.orf1:2000SEP08 195 LI:1166315.1:2000SEP08 448 LI:1166315.1.orf3:2000SEP08 196 LI:204626.1:2000SEP08 449 LI:204626.1.orf1:2000SEP08 197 LI:801140.1:2000SEP08 450 LI:801140.1.orf1:2000SEP08 198 LI:286639.1:2000SEP08 451 LI:286639.1.orf1:2000SEP08 199 LI:288905.4:2000SEP08 452 LI:288905.4.orf3:2000SEP08 200 LI:332161.1:2000SEP08 453 LI:332161.1.orf3:2000SEP08 201 LI:184867.1:2000SEP08 454 LI:184867.1.orf1:2000SEP08 202 LI:229932.4:2000SEP08 455 LI:229932.4.orf1:2000SEP08 203 LI:1189932.1:2000SEP08 456 LI:1189932.1.orf1:2000SEP08 204 LI:1076689.1:2000SEP08 457 LI:1076689.1.orf1:2000SEP08 205 LI:415181.2:2000SEP08 458 LI:415181.2.orf1:2000SEP08 206 LI:296358.1:2000SEP08 459 LI:296358.1.orf3:2000SEP08 207 LI:205186.3:2000SEP08 460 LI:205186.3.orf2:2000SEP08 208 LI:220537.2:2000SEP08 461 LI:220537.2.orf3:2000SEP08 209 LI:248364.2:2000SEP08 462 LI:248364.2.orf2:2000SEP08 210 LI:2048338.1:2000SEP08 463 LI:2048338.1.orf3:2000SEP08 211 LI:1185203.8:2000SEP08 464 LI:1185203.8.orf3:2000SEP08 212 LI:021770.3:2000SEP08 465 LI:021770.3.orf2:2000SEP08 213 LI:1185841.1:2000SEP08 466 LI:1185841.1.orf2:2000SEP08 214 LI:1181710.1:2000SEP08 467 LI:1181710.1.orf1:2000SEP08 215 LI:2048959.1:2000SEP08 468 LI:2048959.1.orf3:2000SEP08 216 LI:798494.1:2000SEP08 469 LI:798494.1.orf3:2000SEP08 217 LI:2049223.1:2000SEP08 470 LI:2049223.1.orf1:2000SEP08 218 LI:1177833.1:2000SEP08 471 LI:1177833.1.orf3:2000SEP08 219 LI:2049267.1:2000SEP08 472 LI:2049267.1.orf3:2000SEP08 220 LI:1165939.1:2000SEP08 473 LI:1165939.1.orf1:2000SEP08 221 LI:1170958.1:2000SEP08 474 LI:1170958.1.orf1:2000SEP08 222 LI:1089827.1:2000SEP08 475 LI:1089827.1.orf2:2000SEP08 223 LI:792112.1:2000SEP08 476 LI:792112.1.orf2:2000SEP08 224 LI:282219.2:2000SEP08 477 LI:282219.2.orf3:2000SEP08 225 LI:1088010.2:2000SEP08 478 LI:1088010.2.orf3:2000SEP08 226 LI:1165276.1:2000SEP08 479 LI:1165276.1.orf3:2000SEP08 227 LI:1169524.2:2000SEP08 480 LI:1169524.2.orf1:2000SEP08 228 LI:1180255.1:2000SEP08 481 LI:1180255.1.orf1:2000SEP08 229 LI:1091903.1:2000SEP08 482 LI:1091903.1.orf2:2000SEP08 230 LI:1169219.1:2000SEP08 483 LI:1169219.1.orf1:2000SEP08 231 LI:2050313.1:2000SEP08 484 LI:2050313.1.orf2:2000SEP08 232 LI:209351.3:2000SEP08 485 LI:209351.3.orf2:2000SEP08 232 LI:209351.3:2000SEP08 486 LI:209351.3.orf3:2000SEP08 233 LI:119900.1:2000SEP08 487 LI:119900.1.orf2:2000SEP08 234 LI:2052274.1:2000SEP08 488 LI:2052274.1.orf1:2000SEP08 235 LI:1075502.1:2000SEP08 489 LI:1075502.1.orf2:2000SEP08 236 LI:813697.1:2000SEP08 490 LI:813697.1.orf3:2000SEP08 237 LI:814261.1:2000SEP08 491 LI:814261.1.orf3:2000SEP08 238 LI:775334.1:2000SEP08 492 LI:775334.1.orf1:2000SEP08 239 LI:1180325.1:2000SEP08 493 LI:1180325.1.orf3:2000SEP08 240 LI:1183147.3:2000SEP08 494 LI:1183147.3.orf2:2000SEP08 241 LI:1175373.3:2000SEP08 495 LI:1175373.3.orf2:2000SEP08 242 LI:813757.1:2000SEP08 496 LI:813757.1.orf1:2000SEP08 243 LI:1182979.2:2000SEP08 497 LI:1182979.2.orf3:2000SEP08 244 LI:1177823.2:2000SEP08 498 LI:1177823.2.orf2:2000SEP08 245 LI:1174279.1:2000SEP08 499 LI:1174279.1.orf3:2000SEP08 246 LI:1178411.1:2000SEP08 500 LI:1178411.1.orf1:2000SEP08 247 LI:1182739.1:2000SEP08 501 LI:1182739.1.orf3:2000SEP08 248 LI:234937.4:2000SEP08 502 LI:234937.4.orf1:2000SEP08 249 LI:1170660.1:2000SEP08 503 LI:1170660.1.orf2:2000SEP08 250 LI:1144409.1:2000SEP08 504 LI:1144409.1.orf1:2000SEP08 251 LI:246290.10:2000SEP08 505 LI:246290.10.orf1:2000SEP08 252 LI:280034.1:2000SEP08 506 LI:280034.1.orf2:2000SEP08

[0301] TABLE 2 SEQ ID NO: Template ID GI Number Probability Score Annotation 1 LG:150318.1:2000SEP08 g11643581 0 Homo sapiens PR- domain containing protein 14 (PRDM14) mRNA, 2 LG:022529.1:2000SEP08 g10047272 0 Homo sapiens mRNA for KIAA1599 protein, partial cds. 3 LG:352559.1:2000SEP08 g13560887 1.00E−11 Homo sapiens EZFIT- related protein 1 mRNA, complete 4 LG:175223.1:2000SEP08 g10433955 1.00E−43 (fl)(Homo sapiens) unnamed protein 5 LG:476989.1:2000SEP08 g12407394 0 Homo sapiens tripartite motif protein TRIM7 (TRIM7) mRNA, 6 LG:253268.7:2000SEP08 g12239368 0 Homo sapiens LYST- interacting protein LIP9 mRNA, partial 7 LG:401322.1:2000SEP08 g13623682 5.00E−26 Homo sapiens, tubulin alpha 1, clone MGC: 2321, 8 LG:1328436.1:2000SEP08 g4589587 2.00E−55 Homo sapiens mRNA for KIAA0972 protein, complete 9 LG:475404.1:2000SEP08 g10434194 0 Homo sapiens cDNA FLJ12606 fis, clone NT2RM4001483, moderately similar 10 LG:1384132.1:2000SEP08 g14042849 1.00E−71 Homo sapiens cDNA FLJ14959 fis, clone PLACE4000156, moderately similar 11 LG:410804.18:2000SEP08 g13543325 3.00E−74 Homo sapiens, hypothetical protein MGC8407, clone MGC: 1820, mRNA, complete 12 LG:1082306.1:2000SEP08 g13325336 0 Homo sapiens, clone MGC: 10520, mRNA, complete 13 LG:233814.4:2000SEP08 g10434873 1.00E−166 Homo sapiens cDNA FLJ13044 fis, clone NT2RP3001355, weakly similar to TRICARBOXYLATE TRANSPORT 14 LG:977478.5:2000SEP08 g12698000 0 Homo sapiens mRNA for KIAA1728 protein, partial cds. 15 LG:025931.1:2000SEP08 g10436359 0 Homo sapiens cDNA FLJ14011 fis, clone Y79AA1002472, weakly similar to 16 LG:885368.1:2000SEP08 g440824 9.00E−60 (fl)(Arabidopsis thaliana) ribosomal 17 LG:1054900.1:2000SEP08 g12052982 0 Homo sapiens mRNA; cDNA DKFZp434l1610 (from clone DKFZp434l1610); 18 LG:995186.2:2000SEP08 g12052982 0 Homo sapiens mRNA; cDNA DKFZp434l1610 (from clone DKFZp434l1610); 19 LG:435048.23:2000SEP08 g10432866 1.00E−177 Homo sapiens cDNA FLJ11583 fis, clone HEMBA1003680, weakly similar to PUTATIVE AMINOPEPTIDASE ZK353.6 IN 20 LG:954859.1:2000SEP08 g10438224 1.00E−176 Homo sapiens cDNA: FLJ21990 fis, clone HEP06386. 21 LG:364370.1:2000SEP08 g14043150 1.00E−163 Homo sapiens, ribosomal protein L13, clone MGC: 15490, mRNA, 22 LG:1098789.1:2000SEP08 g14029703 1.00E−137 Homo sapiens myosin regulatory light chain 2 (MRLC2) mRNA, 23 LG:201540.2:2000SEP08 g12407386 0 Homo sapiens tripartite motif protein TRIM5 isoform delta (TRIM5) mRNA, 24 LG:1077357.1:2000SEP08 g10436361 4.00E−66 Homo sapiens cDNA FLJ14012 fis, clone Y79AA1002482, moderately similar 25 LG:1048846.4:2000SEP08 g10439974 1.00E−154 Homo sapiens cDNA: FLJ23327 fis, clone HEP12630, highly similar to HSZNF37 Homo sapiens ZNF37A 26 LG:336685.1:2000SEP08 g12697317 0 Homo sapiens partial mRNA for 27 LG:1076253.1:2000SEP08 g7959276 5.00E−34 Homo sapiens mRNA for KIAA1508 protein, partial cds. 28 LG:1400601.2:2000SEP08 g14042292 0 Homo sapiens cDNA FLJ14636 fis, clone NT2RP2001233, weakly similar to 29 LG:1079092.3:2000SEP08 g12052982 6.00E−07 Homo sapiens mRNA; cDNA DKFZp434l1610 (from clone DKFZp434l1610); 30 LG:1086064.1:2000SEP08 g10436361 3.00E−76 Homo sapiens cDNA FLJ14012 fis, clone Y79AA1002482, moderately similar 31 LG:1400608.1:2000SEP08 g12052731 1.00E−175 Homo sapiens mRNA; cDNA DKFZp761G18121 (from clone DKFZp761G18121); 32 LG:399275.5:2000SEP08 g14042034 0 Homo sapiens cDNA FLJ14486 fis, clone MAMMA1002650, weakly similar to 33 LG:293943.1:2000SEP08 g7022603 2.00E−24 (fl)(Homo sapiens) unnamed protein 34 LG:345884.1:2000SEP08 g13591711 0 Homo sapiens immunoglobulin receptor translocation associated protein 2b (IRTA2) mRNA, 35 LG:400967.1:2000SEP08 g10047182 1.00E−176 Homo sapiens mRNA for KIAA1559 protein, partial cds. 36 LG:024556.6:2000SEP08 g11999276 0 Homo sapiens solute carrier (SLC25A18) mRNA, complete cds; nuclear gene for 37 LG:081189.3:2000SEP08 g14325768 0 Homo sapiens mRNA for KIAA1776 protein (fibrillin3), 38 LG:018258.1:2000SEP08 g12832288 3.00E−97 0(Mus musculus) 39 LG:450399.3:2000SEP08 g13097599 1.00E−10 Homo sapiens, Similar to ribosomal protein L23, clone IMAGE: 3606198, 40 LG:451122.1:2000SEP08 g6002102 2.00E−38 (fl)(Digitalis lanata) Acyl-CoA binding protein (ACBP) 41 LG:451682.1:2000SEP08 g8671496 1.00E−134 (fl)(Oryza sativa) alpha 3 subunit of 20S proteasome 42 LG:238631.4:2000SEP08 g12803994 0 Homo sapiens, Similar to HLA class II region expressed gene KE2, clone MGC: 4178, mRNA, 43 LG:236654.1:2000SEP08 g11558487 2.00E−08 Homo sapiens mRNA for B-cell lymphoma/leukaemia 11B (BCL11B 44 LG:332655.1:2000SEP08 g12856559 7.00E−93 0(Mus musculus) 45 LG:217396.2:2000SEP08 g10047294 0 Homo sapiens mRNA for KIAA1610 protein, partial cds. 46 LG:090574.1:2000SEP08 g12845416 5.00E−37 0(Mus musculus) 47 LG:202943.1:2000SEP08 g12060829 0 Homo sapiens serologically defined breast cancer antigen NY- BR-38 mRNA, 48 LG:236928.1:2000SEP08 g14388574 0 Macaca fascicularis brain cDNA clone: QtrA- 49 LG:215169.2:2000SEP08 g790349 1.00E−22 Homo sapiens (clone NE68) gene 50 LG:410726.1:2000SEP08 g9963805 2.00E−17 Homo sapiens zinc finger protein ZNF287 (ZNF287) 51 LG:234372.2:2000SEP08 g10436854 0 Homo sapiens cDNA: FLJ20896 fis, clone ADKA03527. 52 LG:022629.1:2000SEP08 g13879442 1.00E−178 (fl)(Mus musculus) Similar to RIKEN cDNA 2310035M22 53 LG:068682.1:2000SEP08 g13898616 0 Homo sapiens serine/threonine protein kinase SSTK (SSTK) mRNA. 54 LG:222335.1:2000SEP08 g14250137 0 Homo sapiens, Similar to RIKEN cDNA 5730421E18 gene, clone 55 LG:331342.1:2000SEP08 g10434081 0 Homo sapiens cDNA FLJ12538 fis, clone NT2RM4000356, moderately similar to RAS-RELATED 56 LG:021770.1:2000SEP08 g9408105 2.00E−47 Homo sapiens dNT- 2 gene for mitochondrial 5′(3′) deoxyribonucleotid 57 LG:181607.9:2000SEP08 g12834244 8.00E−91 0(Mus musculus) 58 LG:1042768.1:2000SEP08 g13937982 1.00E−180 Homo sapiens, translocase of inner mitochondrial membrane 17 (yeast) homolog A, clone MGC: 14756, 59 LG:282729.1:2000SEP08 g12314268 1.00E−107 (5′ incom)(Homo sapiens) dJ14N1.2 (novel S-100/ICaBP type calcium binding domain 60 LG:998305.3:2000SEP08 g12053098 6.00E−88 Homo sapiens mRNA; cDNA DKFZp434A171 (from clone DKFZp434A171); 61 LG:1135213.1:2000SEP08 g6692607 2.00E−69 (fl)(Mus musculus) MGA protein 62 LG:267762.1:2000SEP08 g12854977 1.00E−135 0(Mus musculus) 63 LG:120744.1:2000SEP08 g12052773 0 Homo sapiens mRNA; cDNA DKFZp564B052 (from clone DKFZp564B052); 64 LG:403409.1:2000SEP08 g8896163 0 Homo sapiens kinesin-like protein GAKIN mRNA, 65 LG:226874.3:2000SEP08 g3688393 3.00E−05 Homo sapiens mRNA for triple LIM 66 LG:1045521.4:2000SEP08 g10436742 4.00E−58 Homo sapiens cDNA FLJ14310 fis, clone 67 LG:275876.1:2000SEP08 g5912051 6.00E−30 (3′ and 5′ incom)(Homo sapiens) 68 LG:475127.7:2000SEP08 g7294107 6.00E−44 (fl)(Drosophila melanogaster) CG4638 gene 69 LG:157263.1:2000SEP08 g3047402 3.00E−40 (fl)(Homo sapiens) monocarboxylate transporter 2 70 LG:247382.7:2000SEP08 g4240292 5.00E−25 Homo sapiens mRNA for KIAA0902 protein, complete 71 LG:197367.5:2000SEP08 g10172680 7.00E−14 (fl)(Bacillus halodurans) stage V sporulation protein C (peptidyl- 72 LG:218090.5:2000SEP08 g9295344 0 Homo sapiens HSKM-B (HSKM-B) mRNA, complete 73 LG:216612.4:2000SEP08 g8655677 0 Homo sapiens mRNA; cDNA DKFZp547M236 (from clone 74 LG:197614.1:2000SEP08 g13358641 0 Macaca fascicularis brain 75 LG:378428.1:2000SEP08 g7264026 0 (fl)(Homo sapiens) dJ876B10.2 (novel protein (ortholog of 76 LG:286639.1:2000SEP08 g13383264 0 Homo sapiens mRNA for actin related protein, 77 LG:389870.1:2000SEP08 g14388335 9.00E−63 Macaca fascicularis brain cDNA clone: QflA- 78 LG:1387485.6:2000SEP08 g10435209 0 Homo sapiens cDNA FLJ13261 fis, clone OVARC1000885, weakly similar to OXIDOREDUCTASE 79 LG:230151.1:2000SEP08 g8655647 0 Homo sapiens mRNA; cDNA DKFZp762M115 (from clone 80 LG:215158.5:2000SEP08 g10440162 0 Homo sapiens cDNA: FLJ23465 fis, clone HSI10904. 81 LG:235840.1:2000SEP08 g14042343 0 Homo sapiens cDNA FLJ14666 fis, clone NT2RP2003000, weakly similar to TUMOR NECROSIS FACTOR, ALPHA- 82 LG:350272.1:2000SEP08 g13477234 0 Homo sapiens, Similar to RIKEN cDNA 0610037N03 gene, clone 83 LG:232190.1:2000SEP08 g10434968 1.00E−143 Homo sapiens cDNA FLJ13105 fis, clone NT2RP3002351, weakly similar to Human mRNA for NAD-dependent methylene tetrahydrofolate 84 LG:1068127.1:2000SEP08 g10436724 1.00E−140 Homo sapiens cDNA FLJ14297 fis, clone 85 LG:408751.3:2000SEP08 g8886024 0 Homo sapiens collapsin response mediator protein-5 (CRMP5) mRNA, 86 LG:1078933.1:2000SEP08 g14042843 0 Homo sapiens cDNA FLJ14954 fis, clone PLACE3000169, weakly similar to 87 LG:958731.1:2000SEP08 g9758769 6.00E−88 (fl) (Arabidopsis thaliana) 11-beta- hydroxysteroid 88 LG:024125.5:2000SEP08 g12052958 0 Homo sapiens mRNA; cDNA DKFZp566J2046 (from clone DKFZp566J2046); 89 LG:373637.3:2000SEP08 g11118740 0 Homo sapiens UGT1 gene locus, complete 90 LG:1053229.1:2000SEP08 g12804322 0 Homo sapiens, clone MGC: 4054, mRNA, complete 91 LG:248364.1:2000SEP08 g12847599 0 0(Mus musculus) 92 LG:477130.1:2000SEP08 g6650751 1.00E−55 (fl)(Ceratopteris richardii) ribosomal 93 LG:113786.17:2000SEP08 g10440515 0 Homo sapiens mRNA for FLJ00106 protein, partial cds. 94 LG:347635.1:2000SEP08 g11527996 0 Homo sapiens NOTCH2 protein (NOTCH2) mRNA, 95 LG:242966.4:2000SEP08 g9955987 0 Homo sapiens clone TCCCIA00164 96 LG:217814.1:2000SEP08 g10438977 0 Homo sapiens cDNA: FLJ22551 fis, clone HSI00804. 97 LG:476452.1:2000SEP08 g4126809 1.00E−121 (fl)(Oryza sativa) glyoxalase I 98 LG:1100657.1:2000SEP08 g340298 1.00E−107 Human vasopressin mRNA, complete 99 LG:1132418.2:2000SEP08 g12653472 2.00E−86 Homo sapiens, proteasome (prosome, macropain) subunit, beta type, 100 LG:1098570.1:2000SEP08 g35069 1.00E−171 H. sapiens RNA for nm23-H2 gene. 101 LG:1097987.1:2000SEP08 g9368838 0 Homo sapiens mRNA; cDNA DKFZp547l014 (from clone 102 LG:337818.2:2000SEP08 g14042395 0 Homo sapiens cDNA FLJ14699 fis, clone NT2RP2006571, moderately similar to CYTOCHROME 103 LG:1040582.1:2000SEP08 g13529277 1.00E−119 Homo sapiens, aldo-keto reductase family 1, member A1 (aldehyde reductase), clone 104 LG:1099122.1:2000SEP08 g13097716 8.00E−86 Homo sapiens, guanine nucleotide binding protein (G protein), gamma 5, clone 105 LG:1327449.1:2000SEP08 g14042109 2.00E−96 Homo sapiens cDNA FLJ14531 fis, clone NT2RM2000371, weakly similar to POLYRIBONUCLEOTIDE 106 LG:227933.5:2000SEP08 g9280028 0 Macaca fascicularis brain 107 LG:1043709.2:2000SEP08 g12804588 4.00E−30 Homo sapiens, Similar to CG9172 gene product, clone MGC: 886, 108 LG:1099871.1:2000SEP08 g12652698 1.00E−154 Homo sapiens, purine-rich element binding protein B, clone MGC: 1947, 109 LG:1399139.4:2000SEP08 g10437077 0 Homo sapiens cDNA: FLJ21069 fis, clone CAS01594. 110 LG:236386.1:2000SEP08 g13477131 6.00E−87 (fl)(Homo sapiens) SH3 and PX domain-containing 111 LG:1015157.1:2000SEP08 g1881781 5.00E−72 glyoxalase I (human, HeLa cells, mRNA Partial, 572 112 LG:1065433.1:2000SEP08 g4589587 8.00E−29 Homo sapiens mRNA for KIAA0972 protein, complete 113 LG:236992.4:2000SEP08 g12248381 0 Homo sapiens mRNA for SEMB, 114 LG:1071124.1:2000SEP08 g13543418 0 Homo sapiens, Similar to zinc finger protein 304, clone MGC: 4079, mRNA, 115 LG:206425.2:2000SEP08 g12052883 2.00E−90 Homo sapiens mRNA; cDNA DKFZp564C2478 (from clone DKFZp564C2478); 116 LG:885747.2:2000SEP08 g12804504 2.00E−49 Homo sapiens, Similar to ribosomal protein L31, clone MGC: 1641, mRNA, 117 LG:1140501.1:2000SEP08 g12052919 0 Homo sapiens mRNA; cDNA DKFZp564l1782 (from clone DKFZp564l1782); 118 LG:001239.1:2000SEP08 g14164612 0 Homo sapiens sialic acid binding immunoglobulin- like lectin 10 119 LG:018980.1:2000SEP08 g10435149 0 Homo sapiens cDNA FLJ13220 fis, clone NT2RP4002047, moderately similar to GTP-BINDING 120 LG:1083120.3:2000SEP08 g515786 3.00E−66 H. sapiens (MAR7) chromosome 19 DNA, 302bp. 121 LG:233258.3:2000SEP08 g10433125 0 Homo sapiens cDNA FLJ11790 fis, clone 122 LG:999062.1:2000SEP08 g9759463 3.00E−60 (fl)(Arabidopsis thaliana) 40S 123 LG:887776.1:2000SEP08 g342294 1.00E−66 Macaca mulatta serum albumin 124 LG:1400301.2:2000SEP08 g12751104 1.00E−23 Homo sapiens PNAS-130 mRNA, 125 LG:1329362.1:2000SEP08 g14042849 0 Homo sapiens cDNA FLJ14959 fis, clone PLACE4000156, moderately similar 126 LG:1096498.1:2000SEP08 g13097206 1.00E−110 Homo sapiens, ribosomal protein, large, P1, clone MGC: 5215, mRNA, 127 LG:1096337.1:2000SEP08 g13097206 1.00E−121 Homo sapiens, ribosomal protein, large, P1, clone MGC: 5215, mRNA, 128 LG:1400579.1:2000SEP08 g10437945 4.00E−61 Homo sapiens cDNA: FLJ21781 fis, clone HEP00223. 129 LG:1080091.1:2000SEP08 g10436724 1.00E−154 Homo sapiens cDNA FLJ14297 fis, clone 130 LG:1082203.1:2000SEP08 g10439929 0 Homo sapiens cDNA: FLJ23296 fis, clone HEP10656. 131 LG:1084051.1:2000SEP08 g6807586 1.00E−104 Novel human gene mapping to chomosome 1. 132 LG:1082393.1:2000SEP08 g10954043 0 Homo sapiens KRAB zinc finger protein ZFQR 133 LG:1086183.1:2000SEP08 g12655164 6.00E−58 Homo sapiens, zinc finger protein 256, clone MGC: 1413, mRNA, complete 134 LG:1090268.1:2000SEP08 g13938479 0 Homo sapiens, Similar to hypothetical protein FLJ22301, clone 135 LG:1400597.5:2000SEP08 g14250145 1.00E−156 Homo sapiens, hypothetical protein FLJ23407, clone MGC: 14819, mRNA, complete 136 LG:1080307.2:2000SEP08 g14043840 2.00E−34 Homo sapiens, clone MGC: 14429, mRNA, complete 137 LG:1400603.2:2000SEP08 g4589565 4.00E−31 Homo sapiens mRNA for KIAA0961 protein, complete 138 LG:1052984.1:2000SEP08 g13937998 0 Homo sapiens, Similar to DNA- binding protein, clone MGC: 14780, 139 LG:1091259.1:2000SEP08 g10436675 0 Homo sapiens cDNA FLJ14260 fis, clone PLACE1001118. weakly similar to 140 LG:1082263.2:2000SEP08 g13560887 5.00E−13 Homo sapiens EZFIT- related protein 1 mRNA, complete 141 LG:1048604.2:2000SEP08 g14249843 6.00E−67 Homo sapiens, Similar to hypothetical protein FLJ23233, clone MGC: 14876, 142 LG:1085254.3:2000SEP08 g10437559 0 Homo sapiens cDNA: FLJ21457 fis, clone COL04705. 143 LG:1400606.2:2000SEP08 g14042549 9.00E−54 Homo sapiens cDNA FLJ14779 fis, clone NT2RP4000398, moderately similar 144 LG:1090358.2:2000SEP08 g10047182 6.00E−30 Homo sapiens mRNA for KIAA1559 protein, partial cds. 145 LG:1079064.2:2000SEP08 g10434649 0 Homo sapiens cDNA FLJ12895 fis, clone NT2RP2004187, weakly similar to 146 LG:1076866.1:2000SEP08 g10436460 0 Homo sapiens cDNA FLJ14087 fis, clone MAMMA1000183, weakly similar to 147 LG:969359.1:2000SEP08 g13279004 1.00E−120 Homo sapiens, ferritin, light polypeptide, clone MGC: 10465, mRNA, 148 LG:366783.1:2000SEP08 g9651703 0 Homo sapiens carboxypeptidase B precursor (CPAH) mRNA, complete 149 LG:332176.3:2000SEP08 g13365900 0 Macaca fascicularis brain cDNA clone: QflA- 150 LG:994938.1:2000SEP08 g7023331 1.00E−76 Homo sapiens cDNA FLJ10961 fis, clone PLACE1000588, highly similar to INTERFERON- 151 LG:982800.1:2000SEP08 g12053280 0 Homo sapiens mRNA; cDNA DKFZp434J037 (from clone DKFZp434J037); 152 LG:977850.7:2000SEP08 g10436959 5.00E−64 Homo sapiens cDNA: FLJ20984 fis, clone CAE00871. 153 LG:234748.2:2000SEP08 g13182754 0 Homo sapiens HPHRP mRNA, 154 LG:306284.1:2000SEP08 g14043648 0 Homo sapiens, clone MGC: 14161, mRNA, complete 155 LI:333170.3:2000SEP08 g12314083 1.00E−93 (fl)(Homo sapiens) dJ1007G16.5 (novel high-mobility group (nonhistone chromosomal) 156 LI:336685.2:2000SEP08 g12697317 0 Homo sapiens partial mRNA for 157 LI:279013.5:2000SEP08 g12840673 3.00E−55 0(Mus musculus) 158 LI:1037075.1:2000SEP08 g11342540 0 Homo sapiens mRNA for putative white family ATP- binding cassette transporter (ABCG4 159 LI:1073403.1:2000SEP08 g12804680 9.00E−63 Homo sapiens, S100 calcium- binding protein, beta (neural), clone MGC: 1323, 160 LI:1075296.1:2000SEP08 g12803084 1.00E−112 Homo sapiens, mitochondrial ribosomal protein L12, clone MGC: 8610, mRNA, 161 LI:1085501.1:2000SEP08 g12653784 1.00E−140 Homo sapiens, clone IMAGE: 3349601, 162 LI:1086181.1:2000SEP08 g3043444 1.00E−146 Homo sapiens mRNA for EDF-1 163 LI:1164493.1:2000SEP08 g13436439 0 Homo sapiens, clone MGC: 4400, mRNA, complete 164 LI:1175097.1:2000SEP08 g13937908 4.00E−45 Homo sapiens, Similar to KIAA0961 protein, clone MGC: 12515, mRNA, 165 LI:1092948.1:2000SEP08 g12804414 2.00E−49 Homo sapiens, Similar to hypothetical protein FLJ10891, clone MGC: 925, 166 LI:380378.2:2000SEP08 g8655612 3.00E−79 Homo sapiens mRNA; cDNA DKFZp762O1415 (from clone 167 LI:1029674.1:2000SEP08 g9651088 4.00E−07 Macaca fascicularis brain 168 LI:2048601.3:2000SEP08 g10434880 1.00E−106 Homo sapiens cDNA FLJ13048 fis, clone NT2RP3001399, weakly similar to 169 LI:1186208.1:2000SEP08 g12052731 1.00E−175 Homo sapiens mRNA; cDNA DKFZp761G18121 (from clone DKFZp761G18121); 170 LI:1170753.1:2000SEP08 g14249995 1.00E−101 Homo sapiens, clone MGC: 12518, mRNA, complete 171 LI:1180908.1:2000SEP08 g14042849 0 Homo sapiens cDNA FLJ14959 fis, clone PLACE4000156, moderately similar 172 LI:1182900.2:2000SEP08 g10047304 0 Homo sapiens mRNA for KIAA1615 protein, partial cds. 173 LI:1169548.2:2000SEP08 g14017832 0 Homo sapiens mRNA for KIAA1808 protein, partial cds. 174 LI:1039974.1:2000SEP08 g13366083 0 Homo sapiens MARKL1 mRNA for MAP/microtubule affinity-regulating kinase like 1, 175 LI:1175765.2:2000SEP08 g13752753 5.00E−16 Homo sapiens zinc finger 1111 mRNA, complete cds. 176 LI:313948.1:2000SEP08 g9651098 0 Macaca fascicularis brain 177 LI:335923.2:2000SEP08 g11990770 3.00E−73 (fl)(Homo sapiens) bA534G20.1.1 (novel protein similar to Lysozyme C-1 (1,4-beta-N- acylmuramidase C, 178 LI:345884.1:2000SEP08 g13591713 0 Homo sapiens immunoglobulin receptor translocation associated protein 2c (IRTA2) mRNA, 179 LI:417127.1:2000SEP08 g12652726 1.00E−66 Homo sapiens, clone IMAGE: 3352566, 180 LI:451710.1:2000SEP08 g13899057 1.00E−61 (fl)(Mercurialis annua) ribosomal 181 LI:406882.2:2000SEP08 g7019948 2.00E−57 Homo sapiens cDNA FLJ20081 fis, clone COL03242. 182 LI:728223.1:2000SEP08 g2624328 2.00E−44 (fl)(Oryza sativa) 183 LI:289783.19:2000SEP08 g12654714 0 Homo sapiens, Similar to glucose regulated protein, 58 kDa, clone 184 LI:235255.8:2000SEP08 g12597311 0 Homo sapiens clone IMAGE: 72154 tRNA-guanine transglycosylase (TGT) mRNA, 185 LI:237693.5:2000SEP08 g12406772 4.00E−52 (fl)(Homo sapiens) unnamed protein 186 LI:433670.3:2000SEP08 g14133250 0 Homo sapiens mRNA for KIAA1479 protein, partial cds. 187 LI:202943.4:2000SEP08 g12060829 0 Homo sapiens serologically defined breast cancer antigen NY- BR-38 mRNA, 188 LI:068682.1:2000SEP08 g13540325 0 Homo sapiens serine/threonine kinase FKSG82 (FKSG82) mRNA, 189 LI:203301.3:2000SEP08 g10047160 0 Homo sapiens mRNA for KIAA1548 protein, partial cds. 190 LI:020726.3:2000SEP08 g12834087 1.00E−157 0(Mus musculus) 191 LI:027209.1:2000SEP08 g13159480 1.00E−127 (fl)(Homo sapiens) Translation may initiate at the ATG codon at nucleotides 40-42 192 LI:108819.1:2000SEP08 g12052773 0 Homo sapiens mRNA; cDNA DKFZp564B052 (from clone DKFZp564B052); 193 LI:021759.1:2000SEP08 g12006103 0 Homo sapiens IRA1 mRNA, complete cds, alternatively 194 LI:1165967.1:2000SEP08 g13529103 1.00E−172 Homo sapiens, ribosomal protein S27a, clone MGC: 12414, mRNA, 195 LI:1166315.1:2000SEP08 g12653800 1.00E−116 Homo sapiens, peptidylprolyl isomerase A (cyclophilin A), clone MGC: 2351, 196 LI:204626.1:2000SEP08 g12844770 1.00E−138 0(Mus musculus) 197 LI:801140.1:2000SEP08 g12804322 0 Homo sapiens, clone MGC: 4054, mRNA, complete 198 LI:286639.1:2000SEP08 g13938318 0 Homo sapiens, clone MGC: 15664, mRNA, complete 199 LI:288905.4:2000SEP08 g12698056 0 Homo sapiens mRNA for KIAA1756 protein, partial cds. 200 LI:332161.1:2000SEP08 g14388335 2.00E−62 Macaca fascicularis brain cDNA clone: QflA- 201 LI:184867.1:2000SEP08 g7209586 4.00E−47 (fl)(Rattus norvegicus) DA41 202 LI:229932.4:2000SEP08 g10438187 0 Homo sapiens cDNA: FLJ21963 fis, clone HEP05583. 203 LI:1189932.1:2000SEP08 g12483887 0 Homo sapiens solute carrier 19A3 mRNA, complete 204 LI:1076689.1:2000SEP08 g12804758 6.00E−20 Homo sapiens, ribonuclease 6 precursor, clone MGC: 3554, mRNA, 205 LI:415181.2:2000SEP08 g11762100 0 (fl)(Zea mays) myoinositol 1- 206 LI:296358.1:2000SEP08 g12053148 0 Homo sapiens mRNA; cDNA DKFZp434G2226 (from clone DKFZp434G2226); 207 LI:205186.3:2000SEP08 g567232 4.00E−17 (fl)(Mus musculus) proline-rich protein 208 LI:220537.2:2000SEP08 g13365896 0 Macaca fascicularis brain cDNA clone: QflA- 209 LI:248364.2:2000SEP08 g12847599 0 0(Mus musculus) 210 LI:2048338.1:2000SEP08 g12848905 3.00E−78 0(Mus musculus) 211 LI:1185203.8:2000SEP08 g11231084 3.00E−85 Macaca fascicularis brain 212 LI:021770.3:2000SEP08 g5931541 2.00E−45 Homo sapiens genomic DNA, chromosome 22q11.2, BCRL2 213 LI:1185841.1:2000SEP08 g14269501 0 Homo sapiens unconventional myosin 1G valine form (MYO1G) mRNA, MYO1G-V 214 LI:1181710.1:2000SEP08 g7959206 2.00E−49 Homo sapiens mRNA for KIAA1473 protein, partial cds. 215 LI:2048959.1:2000SEP08 g5817101 1.00E−16 Homo sapiens mRNA; cDNA DKFZp434G1621 (from clone 216 LI:798494.1:2000SEP08 g10047182 2.00E−23 Homo sapiens mRNA for KIAA1559 protein, partial cds. 217 LI:2049223.1:2000SEP08 g7959206 2.00E−43 Homo sapiens mRNA for KIAA1473 protein, partial cds. 218 LI:1177833.1:2000SEP08 g12052982 0 Homo sapiens mRNA; cDNA DKFZp434l1610 (from clone DKFZp434l1610); 219 LI:2049267.1:2000SEP08 g515786 6.00E−61 H. sapiens (MAR7) chromosome 19 DNA, 302bp. 220 LI:1165939.1:2000SEP08 g7020753 9.00E−13 Homo sapiens cDNA FLJ20562 fis, clone KAT11992. 221 LI:1170958.1:2000SEP08 g5262556 1.00E−14 Homo sapiens mRNA; cDNA DKFZp569D2231 (from clone DKFZp569D2231); 222 LI:1089827.1:2000SEP08 g14042292 0 Homo sapiens cDNA FLJ14636 fis, clone NT2RP2001233, weakly similar to 223 LI:792112.1:2000SEP08 g10437945 4.00E−61 Homo sapiens cDNA: FLJ21781 fis, clone HEP00223. 224 LI:282219.2:2000SEP08 g12656630 7.00E−63 Homo sapiens Kruppel-like zinc finger protein GLIS2 mRNA, complete 225 LI:1088010.2:2000SEP08 g13623632 0 Homo sapiens, clone MGC: 13105, mRNA, complete 226 LI:1165276.1:2000SEP08 g6807586 1.00E−106 Novel human gene mapping to chomosome 1. 227 LI:1169524.2:2000SEP08 g10047182 5.00E−30 Homo sapiens mRNA for KIAA1559 protein, partial cds. 228 LI:1180255.1:2000SEP08 g14017870 0 Homo sapiens mRNA for KIAA1827 protein, partial cds. 229 LI:1091903.1:2000SEP08 g14042372 2.00E−49 Homo sapiens cDNA FLJ14686 fis, clone NT2RP2004961, moderately similar to Rattus norvegicus KRAB/zinc finger 230 LI:1169219.1:2000SEP08 g13937998 0 Homo sapiens, Similar to DNA- binding protein, clone MGC: 14780, 231 LI:2050313.1:2000SEP08 g12862319 0 Homo sapiens mRNA for WDC146, 232 LI:209351.3:2000SEP08 g14042794 0 Homo sapiens cDNA FLJ14923 fis, clone PLACE1008244, weakly similar to VEGETATIBLE 233 LI:119900.1:2000SEP08 g14042821 2.00E−66 Homo sapiens cDNA FLJ14939 fis, clone PLACE1010702, moderately similar 234 LI:2052274.1:2000SEP08 g8698839 4.00E−07 Homo sapiens genomic DNA, chromosome 8q23, 235 LI:1075502.1:2000SEP08 g13960141 1.00E−114 Homo sapiens, uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine-5′- decarboxylase), 236 LI:813697.1:2000SEP08 g7020744 6.00E−59 Homo sapiens cDNA FLJ20557 fis, clone KAT11869. 237 LI:814261.1:2000SEP08 g7023331 1.00E−76 Homo sapiens cDNA FLJ10961 fis, clone PLACE1000588, highly similar to INTERFERON- 238 LI:775334.1:2000SEP08 g4589587 3.00E−23 Homo sapiens mRNA for KIAA0972 protein, complete 239 LI:1180325.1:2000SEP08 g10438159 0 Homo sapiens cDNA: FLJ21941 fis, clone HEP04524. 240 LI:1183147.3:2000SEP08 g10440084 0 Homo sapiens cDNA: FLJ23407 fis, clone HEP19601. 241 LI:1175373.3:2000SEP08 g7243242 5.00E−51 Homo sapiens mRNA for KIAA1431 protein, partial cds. 242 LI:813757.1:2000SEP08 g4589587 1.00E−31 Homo sapiens mRNA for KIAA0972 protein, complete 243 LI:1182979.2:2000SEP08 g14042292 2.00E−87 Homo sapiens cDNA FLJ14636 fis, clone NT2RP2001233, weakly similar to 244 LI:1177823.2:2000SEP08 g12052982 0 Homo sapiens mRNA; cDNA DKFZp434l1610 (from clone DKFZp434l1610); 245 LI:1174279.1:2000SEP08 g10047182 1.00E−27 Homo sapiens mRNA for KIAA1559 protein, partial cds. 246 LI:1178411.1:2000SEP08 g14042843 0 Homo sapiens cDNA FLJ14954 fis, clone PLACE3000169, weakly similar to 247 LI:1182739.1:2000SEP08 g12655164 8.00E−31 Homo sapiens, zinc finger protein 256, clone MGC: 1413, mRNA, complete 248 LI:234937.4:2000SEP08 g12804418 0 Homo sapiens, clone MGC: 1136, mRNA, complete 249 LI:1170660.1:2000SEP08 g14388419 0 Macaca fascicularis brain cDNA clone: QmoA- 250 LI:1144409.1:2000SEP08 g12053280 0 Homo sapiens mRNA; cDNA DKFZp434J037 (from clone DKFZp434J037); 251 LI:246290.10:2000SEP08 g10438695 0 Homo sapiens cDNA: FLJ22347 fis, clone HRC06188. 252 LI:280034.1:2000SEP08 g12847023 1.00E−132 0(Mus musculus)

[0302] TABLE 3 SEQ ID NO: Template ID Start Stop Frame Pfam Hit Pfam Description E-value 1 LG:150318.1:2000SEP08 11 79 forward 2 zf-C2H2 Zinc finger, C2H2 type 2.00E−06 2 LG:022529.1:2000SEP08 426 701 forward 3 C2 C2 domain 3.30E−06 3 LG:352559.1:2000SEP08 125 313 forward 2 KRAB KRAB box 1.60E−41 4 LG:175223.1:2000SEP08 210 431 forward 3 CSD ‘Cold-shock’ DNA-binding domain 1.40E−18 5 LG:476989.1:2000SEP08 149 223 forward 2 zf-C3HC4 Zinc finger, C3HC4 type (RING finger) 3.00E−10 6 LG:253268.7:2000SEP08 211 435 forward 1 rrm RNA recognition motif. (a.k.a. RRM, 3.50E−16 RBD, or RNP domain) 7 LG:401322.1:2000SEP08 156 341 forward 3 tubulin Tubulin/FtsZ family 7.10E−20 7 LG:401322.1:2000SEP08 371 478 forward 2 tubulin Tubulin/FtsZ family 2.50E−06 8 LG:1328436.1:2000SEP08 134 322 forward 2 KRAB KRAB box 1.70E−42 9 LG:475404.1:2000SEP08 176 328 forward 2 KRAB KRAB box 1.10E−15 10 LG:1384132.1:2000SEP08 157 225 forward 1 zf-C2H2 Zinc finger, C2H2 type 9.00E−04 11 LG:410804.18:2000SEP08 133 243 forward 1 pkinase Protein kinase domain 7.90E−04 12 LG:1082306.1:2000SEP08 199 378 forward 1 KRAB KRAB box 4.90E−20 12 LG:1082306.1:2000SEP08 559 627 forward 1 zf-C2H2 Zinc finger, C2H2 type 9.60E−05 13 LG:233814.4:2000SEP08 624 947 forward 3 mito_carr Mitochondrial carrier protein 2.50E−04 14 LG:977478.5:2000SEP08 351 449 forward 3 ank Ank repeat 1.10E−08 15 LG:025931.1:2000SEP08 660 728 forward 3 zf-C2H2 Zinc finger, C2H2 type 4.50E−06 15 LG:025931.1:2000SEP08 29 97 forward 2 zf-C2H2 Zinc finger, C2H2 type 7.20E−06 16 LG:885368.1:2000SEP08 133 462 forward 1 Ribosomal_S8 Ribosomal protein S8 7.50E−48 17 LG:1054900.1:2000SEP08 78 218 forward 3 KRAB KRAB box 2.30E−17 18 LG:995186.2:2000SEP08 151 357 forward 1 KRAB KRAB box 1.10E−04 19 LG:435048.23:2000SEP08 2 457 forward 2 Peptidase_M17 Cytosol aminopeptidase family, 5.30E−09 catalytic domain 20 LG:954859.1:2000SEP08 245 565 forward 2 Ribosomal_L7Ae Ribosomal protein 7.80E−17 L7Ae/L30e/S12e/Gadd45 family 21 LG:364370.1:2000SEP08 42 578 forward 3 Ribosomal_L13e Ribosomal protein L13e 2.30E−137 22 LG:1098789.1:2000SEP08 45 131 forward 3 efhand EF hand 8.70E−05 23 LG:201540.2:2000SEP08 479 604 forward 2 zf-B_box B-box zinc finger. 9.60E−14 23 LG:201540.2:2000SEP08 254 385 forward 2 zf-C3HC4 Zinc finger, C3HC4 type (RING finger) 4.80E−13 24 LG:1077357.1:2000SEP08 94 282 forward 1 KRAB KRAB box 4.80E−31 25 LG:1048846.4:2000SEP08 60 245 forward 3 KRAB KRAB box 7.10E−39 26 LG:336685.1:2000SEP08 945 1121 forward 3 homeobox Homeobox domain 3.10E−11 27 LG:1076253.1:2000SEP08 6 188 forward 3 KRAB KRAB box 4.10E−14 27 LG:1076253.1:2000SEP08 939 1007 forward 3 zf-C2H2 Zinc finger, C2H2 type 9.30E−06 28 LG:1400601.2:2000SEP08 38 106 forward 2 zf-C2H2 Zinc finger, C2H2 type 1.50E−05 29 LG:1079092.3:2000SEP08 314 382 forward 2 zf-C2H2 Zinc finger, C2H2 type 8.80E−06 30 LG:1086064.1:2000SEP08 128 316 forward 2 KRAB KRAB box 2.00E−34 31 LG:1400608.1:2000SEP08 138 326 forward 3 KRAB KRAB box 1.30E−40 32 LG:399275.5:2000SEP08 328 645 forward 1 BTB BTB/POZ domain 4.10E−18 33 LG:293943.1:2000SEP08 265 327 forward 1 IQ IQ calmodulin-binding motif 5.10E−04 34 LG:345884.1:2000SEP08 203 355 forward 2 ig Immunoglobulin domain 7.40E−04 35 LG:400967.1:2000SEP08 109 300 forward 1 KRAB KRAB box 1.50E−35 36 LG:024556.6:2000SEP08 526 774 forward 1 mito_carr Mitochondrial carrier protein 2.90E−19 37 LG:081189.3:2000SEP08 362 475 forward 2 EGF EGF-like domain 3.80E−06 38 LG:018258.1:2000SEP08 174 605 forward 3 Nitroreductase Nitroreductase family 9.00E−05 39 LG:450399.3:2000SEP08 81 446 forward 3 Ribosomal_L14 Ribosomal protein L14p/L23e 1.20E−53 40 LG:451122.1:2000SEP08 49 303 forward 1 ACBP Acyl CoA binding protein 1.70E−51 41 LG:451682.1:2000SEP08 117 560 forward 3 proteasome Proteasome A-type and B-type 4.40E−59 42 LG:238631.4:2000SEP08 100 453 forward 1 KE2 KE2 family protein 3.80E−38 43 LG:236654.1:2000SEP08 810 878 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.20E−04 43 LG:236654.1:2000SEP08 434 502 forward 2 zf-C2H2 Zinc finger, C2H2 type 6.60E−04 44 LG:332655.1:2000SEP08 415 513 forward 1 ank Ank repeat 3.10E−10 45 LG:217396.2:2000SEP08 679 882 forward 1 ELM2 ELM2 domain 5.00E−14 45 LG:217396.2:2000SEP08 994 1134 forward 1 myb_DNA-binding Myb-like DNA-binding domain 2.00E−11 46 LG:090574.1:2000SEP08 33 245 forward 3 carb_anhydrase Eukaryotic-type carbonic anhydrase 3.10E−31 47 LG:202943.1:2000SEP08 199 360 forward 1 sushi Sushi domain (SCR repeat) 3.80E−18 48 LG:236928.1:2000SEP08 259 1101 forward 1 GNS1_SUR4 GNS1/SUR4 family 9.80E−09 49 LG:215169.2:2000SEP08 89 208 forward 2 Idl_recept_a Low-density lipoprotein receptor 1.00E−12 domain class A 50 LG:410726.1:2000SEP08 724 912 forward 1 KRAB KRAB box 2.10E−17 50 LG:410726.1:2000SEP08 352 636 forward 1 SCAN SCAN domain 8.90E−55 51 LG:234372.2:2000SEP08 557 862 forward 2 PH PH domain 3.00E−09 51 LG:234372.2:2000SEP08 950 1408 forward 2 RhoGAP RhoGAP domain 3.30E−39 51 LG:234372.2:2000SEP08 1952 2119 forward 2 SH3 SH3 domain 4.60E−11 52 LG:022629.1:2000SEP08 261 410 forward 3 zf-C3HC4 Zinc finger, C3HC4 type (RING finger) 2.00E−07 53 LG:068682.1:2000SEP08 176 883 forward 2 pkinase Protein kinase domain 1.70E−65 54 LG:222335.1:2000SEP08 7 732 forward 1 DUF71 Domain of unknown function DUF71 6.70E−83 55 LG:331342.1:2000SEP08 558 1076 forward 3 arf ADP-ribosylation factor family 1.20E−04 55 LG:331342.1:2000SEP08 588 1154 forward 3 ras Ras family 2.60E−79 56 LG:021770.1:2000SEP08 228 1199 forward 3 adh_zinc Zinc-binding dehydrogenases 7.80E−20 57 LG:181607.9:2000SEP08 161 604 forward 2 Josephin Josephin 5.00E−50 58 LG:1042768.1:2000SEP08 42 443 forward 3 Tim17 Mitochondrial import inner membrane 1.40E−82 translocase subunit Tim17 59 LG:282729.1:2000SEP08 61 192 forward 1 S_100 S-100/ICaBP type calcium binding 1.10E−12 domain 60 LG:998305.3:2000SEP08 266 364 forward 2 ank Ank repeat 2.10E−07 61 LG:1135213.1:2000SEP08 340 531 forward 1 T-box T-box 8.80E−27 62 LG:267762.1:2000SEP08 64 1125 forward 1 A_deaminase Adenosine/AMP deaminase 7.80E−20 63 LG:120744.1:2000SEP08 301 813 forward 1 vwa von Willebrand factor type A domain 1.90E−52 64 LG:403409.1:2000SEP08 1458 1652 forward 3 FHA FHA domain 3.00E−04 64 LG:403409.1:2000SEP08 78 1193 forward 3 kinesin Kinesin motor domain 6.80E−172 65 LG:226874.3:2000SEP08 118 291 forward 1 LIM LIM domain 8.40E−13 66 LG:1045521.4:2000SEP08 160 1464 forward 1 aminotran_1 Aminotransferase class-I 2.00E−10 67 LG:275876.1:2000SEP08 508 831 forward 1 CH Calponin homology (CH) domain 2.40E−26 68 LG:475127.7:2000SEP08 169 498 forward 1 GTP_EFTU Elongation factor Tu family 2.20E−46 69 LG:157263.1:2000SEP08 163 1314 forward 1 MCT Monocarboxylate transporter 6.10E−31 70 LG:247382.7:2000SEP08 1105 1353 forward 1 PDZ PDZ domain (Also known as DHR or 4.20E−07 GLGF). 70 LG:247382.7:2000SEP08 487 684 forward 1 SAM SAM domain (Sterile alpha motif) 1.20E−11 71 LG:197367.5:2000SEP08 50 472 forward 2 Pept_tRNA_hydro Peptidyl-tRNA hydrolase 8.90E−05 72 LG:218090.5:2000SEP08 179 295 forward 2 zf-MYND MYND finger 3.00E−10 73 LG:216612.4:2000SEP08 138 1274 forward 3 Cation_efflux Cation efflux family 8.90E−63 74 LG:197614.1:2000SEP08 1699 3048 forward 1 Oxysterol_BP Oxysterol-binding protein 4.10E−31 74 LG:197614.1:2000SEP08 886 1164 forward 1 PH PH domain 1.20E−14 75 LG:378428.1:2000SEP08 621 920 forward 3 PH PH domain 2.00E−06 76 LG:286639.1:2000SEP08 1294 1713 forward 1 actin Actin 9.10E−64 76 LG:286639.1:2000SEP08 630 1319 forward 3 actin Actin 1.70E−62 77 LG:389870.1:2000SEP08 131 640 forward 2 ras Ras family 3.40E−37 78 LG:1387485.6:2000SEP08 227 709 forward 2 adh_short short chain dehydrogenase 1.10E−25 79 LG:230151.1:2000SEP08 631 1602 forward 1 E1_dehydrog Dehydrogenase E1 component 1.10E−09 80 LG:215158.5:2000SEP08 1243 1377 forward 1 zf-AN1 AN1-like Zinc finger 9.10E−04 81 LG:235840.1:2000SEP08 1241 1537 forward 2 K_tetra K+ channel tetramerisation domain 5.60E−22 82 LG:350272.1:2000SEP08 1424 1780 forward 2 SPRY SPRY domain 2.10E−10 82 LG:350272.1:2000SEP08 557 682 forward 2 zf-C3HC4 Zinc finger, C3HC4 type (RING finger) 5.30E−11 83 LG:232190.1:2000SEP08 497 691 forward 2 zf-DHHC DHHC zinc finger domain 2.30E−38 84 LG:1068127.1:2000SEP08 158 307 forward 2 KRAB KRAB box 3.00E−12 85 LG:408751.3:2000SEP08 194 1204 forward 2 Dihydroorotase Dihydroorotase-like 1.20E−12 85 LG:408751.3:2000SEP08 456 1355 forward 3 Dihydroorotase Dihydroorotase-like 6.60E−08 86 LG:1078933.1:2000SEP08 373 441 forward 1 zf-C2H2 Zinc finger, C2H2 type 1.20E−07 86 LG:1078933.1:2000SEP08 689 775 forward 2 zf-C2H2 Zinc finger, C2H2 type 1.00E−03 87 LG:958731.1:2000SEP08 153 707 forward 3 adh_short short chain dehydrogenase 2.40E−39 88 LG:024125.5:2000SEP08 132 635 forward 3 FAA_hydrolase Fumarylacetoacetate (FAA) hydrolase 1.20E−83 family 89 LG:373637.3:2000SEP08 61 255 forward 1 DnaJ DnaJ domain 7.40E−33 90 LG:1053229.1:2000SEP08 514 582 forward 1 zf-C2H2 Zinc finger, C2H2 type 2.50E−08 91 LG:248364.1:2000SEP08 253 594 forward 1 BTB BTB/POZ domain 3.60E−04 91 LG:248364.1:2000SEP08 1544 1612 forward 2 zf-C2H2 Zinc finger, C2H2 type 7.10E−06 92 LG:477130.1:2000SEP08 174 554 forward 3 Ribosomal_L13 Ribosomal protein L13 3.60E−37 93 LG:113786.17:2000SEP08 134 376 forward 2 PDZ PDZ domain (Also known as DHR or 8.10E−15 GLGF). 94 LG:347635.1:2000SEP08 315 410 forward 3 EGF EGF-like domain 6.70E−09 94 LG:347635.1:2000SEP08 605 709 forward 2 EGF EGF-like domain 1.10E−04 94 LG:347635.1:2000SEP08 1057 1152 forward 1 EGF EGF-like domain 1.20E−04 95 LG:242966.4:2000SEP08 7 918 forward 1 aldedh Aldehyde dehydrogenase family 1.10E−05 95 LG:242966.4:2000SEP08 1031 1993 forward 2 aldedh Aldehyde dehydrogenase family 2.20E−05 96 LG:217814.1:2000SEP08 1167 1265 forward 3 ank Ank repeat 6.60E−08 97 LG:476452.1:2000SEP08 210 581 forward 3 Glyoxalase Glyoxalase/Bleomycln resistance 8.10E−39 protein/Dioxygenase superfamily 98 LG:1100657.1:2000SEP08 151 384 forward 1 hormone5 Neurohypophysial hormones, C- 8.60E−47 terminal Domain 99 LG:1132418.2:2000SEP08 109 393 forward 1 proteasome Proteasome A-type and B-type 1.10E−14 100 LG:1098570.1:2000SEP08 129 572 forward 3 NDK Nucleoside diphosphate kinases 3.70E−117 101 LG:1097987.1:2000SEP08 747 908 forward 3 Ribosomal_L23 Ribosomal protein L23 5.80E−14 102 LG:337818.2:2000SEP08 136 1518 forward 1 p450 Cytochrome P450 6.30E−175 103 LG:1040582.1:2000SEP08 266 556 forward 2 aldo_ket_red Aldo/keto reductase family 1.30E−47 103 LG:1040582.1:2000SEP08 546 635 forward 3 aldo_ket_red Aldo/keto reductase family 7.60E−06 104 LG:1099122.1:2000SEP08 84 248 forward 3 G-gamma GGL domain 4.90E−31 105 LG:1327449.1:2000SEP08 461 526 forward 2 Ribosomal_S8 Ribosomal protein S8 4.80E−07 105 LG:1327449.1:2000SEP08 246 359 forward 3 Ribosomal_S8 Ribosomal protein S8 3.00E−06 106 LG:227933.5:2000SEP08 523 1455 forward 1 AMP-binding AMP-binding enzyme 7.20E−05 107 LG:1043709.2:2000SEP08 457 723 forward 1 oxidored_q6 NADH ubiquinone oxidoreductase, 20 Kd 8.40E−08 subunit 108 LG:1099871.1:2000SEP08 34 411 forward 1 histone Core histone H2A/H2B/H3/H4 4.50E−47 109 LG:1399139.4:2000SEP08 117 233 forward 3 CAP_GLY CAP-Gly domain 4.30E−10 110 LG:236386.1:2000SEP08 1383 1712 forward 3 PX PX domain 1.90E−13 111 LG:1015157.1:2000SEP08 115 552 forward 1 Glyoxalase Glyoxalase/Bleomycin resistance 6.00E−38 protein/Dioxygenase superfamily 112 LG:1065433.1:2000SEP08 264 449 forward 3 KRAB KRAB box 1.30E−38 113 LG:236992.4:2000SEP08 286 465 forward 1 Sema Sema domain 2.70E−21 113 LG:236992.4:2000SEP08 209 292 forward 2 Sema Sema domain 3.60E−06 114 LG:1071124.1:2000SEP08 469 630 forward 1 KRAB KRAB box 1.20E−16 115 LG:206425.2:2000SEP08 109 519 forward 1 GBP Guanylate-binding protein, N-terminal 1.60E−100 domain 115 LG:206425.2:2000SEP08 491 916 forward 2 GBP Guanylate-binding protein, N-terminal 2.70E−70 domain 115 LG:206425.2:2000SEP08 1164 1685 forward 3 GBP_C Guanylate-binding protein, C-terminal 3.50E−71 domain 115 LG:206425.2:2000SEP08 920 1201 forward 2 GBP_C Guanylate-binding protein, C-terminal 3.10E−63 domain 115 LG:206425.2:2000SEP08 1651 1773 forward 1 GBP_C Guanylate-binding protein, C-terminal 1.80E−04 domain 116 LG:885747.2:2000SEP08 372 569 forward 3 Ribosomal_L31e Ribosomal protein L31e 9.50E−16 117 LG:1140501.1:2000SEP08 176 340 forward 2 ATP1G1_PLM_(—) ATP1G1/PLM/MAT8 family 9.30E−22 MAT8 118 LG:001239.1:2000SEP08 1686 1850 forward 3 ig Immunoglobulin domain 2.50E−08 118 LG:001239.1:2000SEP08 1391 1561 forward 2 ig Immunoglobulin domain 4.00E−08 119 LG:018980.1:2000SEP08 395 502 forward 2 GTP_EFTU Elongation factor Tu family 3.20E−09 119 LG:018980.1:2000SEP08 634 801 forward 1 GTP_EFTU Elongation factor Tu family 3.50E−07 119 LG:018980.1:2000SEP08 159 215 forward 3 GTP_EFTU Elongation factor Tu family 6.90E−07 120 LG:1083120.3:2000SEP08 117 266 forward 3 KRAB KRAB box 5.10E−22 121 LG:233258.3:2000SEP08 1797 2069 forward 3 cadherin Cadherin domain 3.90E−24 122 LG:999062.1:2000SEP08 78 497 forward 3 Ribosomal_S19e Ribosomal protein S19e 2.10E−101 123 LG:887776.1:2000SEP08 101 625 forward 2 transport_prot Serum albumin family 3.30E−92 123 LG:887776.1:2000SEP08 699 1163 forward 3 transport_prot Serum albumin family 5.90E−41 124 LG:1400301.2:2000SEP08 253 441 forward 1 KRAB KRAB box 2.10E−38 125 LG:1329362.1:2000SEP08 194 262 forward 2 zf-C2H2 Zinc finger, C2H2 type 3.90E−06 126 LG:1096498.1:2000SEP08 17 358 forward 2 60s_ribosomal 60s Acidic ribosomal protein 1.70E−48 127 LG:1096337.1:2000SEP08 512 637 forward 2 60s_ribosomal 60s Acidic ribosomal protein 4.10E−07 127 LG:1096337.1:2000SEP08 619 738 forward 1 60s_ribosomal 60s Acidic ribosomal protein 1.50E−04 128 LG:1400579.1:2000SEP08 200 268 forward 2 zf-C2H2 Zinc finger, C2H2 type 7.80E−05 129 LG:1080091.1:2000SEP08 151 318 forward 1 KRAB KRAB box 1.80E−25 130 LG:1082203.1:2000SEP08 961 1029 forward 1 zf-C2H2 Zinc finger, C2H2 type 2.10E−08 131 LG:1084051.1:2000SEP08 195 263 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.80E−06 132 LG:1082393.1:2000SEP08 237 425 forward 3 KRAB KRAB box 1.80E−36 132 LG:1082393.1:2000SEP08 1251 1319 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.40E−06 133 LG:1086183.1:2000SEP08 308 478 forward 2 KRAB KRAB box 1.50E−15 133 LG:1086183.1:2000SEP08 833 901 forward 2 zf-C2H2 Zinc finger, C2H2 type 9.60E−07 134 LG:1090268.1:2000SEP08 1167 1235 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.00E−07 135 LG:1400597.5:2000SEP08 63 131 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.20E−04 136 LG:1080307.2:2000SEP08 108 239 forward 3 KRAB KRAB box 3.60E−04 137 LG:1400603.2:2000SEP08 299 490 forward 2 KRAB KRAB box 5.50E−41 137 LG:1400603.2:2000SEP08 929 997 forward 2 zf-C2H2 Zinc finger, C2H2 type 1.20E−04 138 LG:1052984.1:2000SEP08 142 330 forward 1 KRAB KRAB box 3.70E−41 139 LG:1091259.1:2000SEP08 555 623 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.20E−07 140 LG:1082263.2:2000SEP08 258 443 forward 3 KRAB KRAB box 2.50E−29 140 LG:1082263.2:2000SEP08 981 1049 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.70E−07 141 LG:1048604.2:2000SEP08 351 530 forward 3 KRAB KRAB box 3.50E−20 142 LG:1085254.3:2000SEP08 746 814 forward 2 zf-C2H2 Zinc finger, C2H2 type 3.10E−07 143 LG:1400606.2:2000SEP08 244 432 forward 1 KRAB KRAB box 7.60E−41 143 LG:1400606.2:2000SEP08 904 972 forward 1 zf-C2H2 Zinc finger, C2H2 type 1.80E−07 144 LG:1090358.2:2000SEP08 385 573 forward 1 KRAB KRAB box 1.30E−47 144 LG:1090358.2:2000SEP08 862 930 forward 1 zf-C2H2 Zinc finger, C2H2 type 7.90E−07 145 LG:1079064.2:2000SEP08 325 612 forward 1 SCAN SCAN domain 3.00E−39 146 LG:1076866.1:2000SEP08 203 391 forward 2 KRAB KRAB box 6.20E−39 146 LG:1076866.1:2000SEP08 1868 1936 forward 2 zf-C2H2 Zinc finger, C2H2 type 5.20E−08 147 LG:969359.1:2000SEP08 221 715 forward 2 ferritin Ferritin 3.10E−86 148 LG:366783.1:2000SEP08 70 609 forward 1 Zn_carbOpept Zinc carboxypeptidase 8.80E−76 148 LG:366783.1:2000SEP08 705 806 forward 3 Zn_carbOpept Zinc carboxypeptidase 2.20E−10 148 LG:366783.1:2000SEP08 623 724 forward 2 Zn_carbOpept Zinc carboxypeptidase 1.80E−05 149 LG:332176.3:2000SEP08 5 1060 forward 2 Glyco_hydro_31 Glycosyl hydrolases family 31 2.40E−163 150 LG:994938.1:2000SEP08 3 95 forward 3 GBP Guanylate-binding protein, N-terminal 4.20E−14 domain 151 LG:982800.1:2000SEP08 16 243 forward 1 pkinase Protein kinase domain 1.30E−10 152 LG:977850.7:2000SEP08 7 102 forward 1 zf-DHHC DHHC zinc finger domain 1.30E−04 153 LG:234748.2:2000SEP08 6 149 forward 3 PTE Phosphotriesterase family 1.20E−19 154 LG:306284.1:2000SEP08 197 613 forward 2 Band_41 FERM domain (Band 4.1 family) 2.00E−52 155 LI:333170.3:2000SEP08 292 498 forward 1 HMG_box HMG (high mobility group) box 1.80E−22 156 LI:336685.2:2000SEP08 913 1092 forward 1 homeobox Homeobox domain 4.20E−15 157 LI:279013.5:2000SEP08 393 500 forward 3 WD40 WD domain, G-beta repeat 2.70E−05 158 LI:1037075.1:2000SEP08 322 666 forward 1 ABC_tran ABC transporter 7.10E−04 158 LI:1037075.1:2000SEP08 328 375 forward 1 PRK Phosphoribulokinase/Uridine kinase 7.40E−04 family 159 LI:1073403.1:2000SEP08 203 289 forward 2 efhand EF hand 5.50E−04 159 LI:1073403.1:2000SEP08 56 187 forward 2 S_100 S-100/CaBP type calcium binding 3.60E−23 domain 160 LI:1075296.1:2000SEP08 337 543 forward 1 Ribosomal_L12 Ribosomal protein L7/L12 C-terminal 5.40E−09 domain 161 LI:1085501.1:2000SEP08 561 776 forward 3 EF1BD EF-1 guanine nucleotide exchange 1.20E−24 domain 162 LI:1086181.1:2000SEP08 305 469 forward 2 HTH_3 Helix-turn-helix 1.20E−10 163 LI:1164493.1:2000SEP08 365 553 forward 2 KRAB KRAB box 8.10E−31 164 LI:1175097.1:2000SEP08 460 648 forward 1 KRAB KRAB box 7.60E−41 165 LI:1092948.1:2000SEP08 446 595 forward 2 KRAB KRAB box 2.80E−21 166 LI:380378.2:2000SEP08 120 419 forward 3 mito_carr Mitochondrial carrier protein 1.30E−25 167 LI:1029674.1:2000SEP08 360 431 forward 3 LRR Leucine Rich Repeat 9.00E−04 168 LI:2048601.3:2000SEP08 2 145 forward 2 ig Immunoglobulin domain 3.00E−05 169 LI:1186208.1:2000SEP08 161 349 forward 2 KRAB KRAB box 1.30E−40 170 LI:1170753.1:2000SEP08 130 318 forward 1 KRAB KRAB box 8.40E−42 171 LI:1180908.1:2000SEP08 509 577 forward 2 zf-C2H2 Zinc finger, C2H2 type 3.90E−06 171 LI:1180908.1:2000SEP08 340 408 forward 1 zf-C2H2 Zinc finger, C2H2 type 1.30E−04 172 LI:1182900.2:2000SEP08 346 414 forward 1 zf-C2H2 Zinc finger, C2H2 type 3.10E−07 173 LI:1169548.2:2000SEP08 393 500 forward 3 VHP Villin headpiece domain 7.10E−20 174 LI:1039974.1:2000SEP08 191 742 forward 2 pkinase Protein kinase domain 1.30E−37 175 LI:1175765.2:2000SEP08 279 446 forward 3 KRAB KRAB box 5.20E−23 176 LI:313948.1:2000SEP08 75 143 forward 3 zf-C2H2 Zinc finger, C2H2 type 2.20E−07 177 LI:335923.2:2000SEP08 215 523 forward 2 lys C-type lysozyme/alpha-lactalbumin 1.60E−42 family 178 LI:345884.1:2000SEP08 208 360 forward 1 ig Immunoglobulin domain 7.40E−04 179 LI:417127.1:2000SEP08 359 529 forward 2 KRAB KRAB box 4.90E−22 180 LI:451710.1:2000SEP08 130 459 forward 1 Ribosomal_L32e Ribosomal protein L32 4.80E−57 181 LI:406882.2:2000SEP08 247 408 forward 1 Kelch Kelch motif 4.20E−11 181 LI:406882.2:2000SEP08 656 793 forward 2 Kelch Kelch motif 8.90E−09 182 LI:728223.1:2000SEP08 158 373 forward 2 rrm RNA recognition motif. (a.k.a. RRM, 1.20E−28 RBD, or RNP domain) 183 LI:289783.19:2000SEP08 821 1003 forward 2 thiored Thioredoxin 1.70E−20 183 LI:289783.19:2000SEP08 747 800 forward 3 thiored Thioredoxin 5.10E−05 184 LI:235255.8:2000SEP08 419 919 forward 2 TGT Queuine tRNA-ribosyltransferase 2.10E−24 184 LI:235255.8:2000SEP08 747 1346 forward 3 TGT Queuine tRNA-ribosyltransferase 7.00E−15 185 LI:237693.5:2000SEP08 48 518 forward 3 abhydrolase_2 Phospholipase/Carboxylesterase 6.20E−07 186 LI:433670.3:2000SEP08 404 682 forward 2 Sema Sema domain 3.80E−26 187 LI:202943.4:2000SEP08 119 223 forward 2 EGF EGF-like domain 1.60E−05 187 LI:202943.4:2000SEP08 1304 1465 forward 2 sushi Sushi domain (SCR repeat) 3.80E−18 188 LI:068682.1:2000SEP08 169 876 forward 1 pkinase Protein kinase domain 1.70E−65 189 LI:203301.3:2000SEP08 570 716 forward 3 Band_41 FERM domain (Band 4.1 family) 1.50E−20 189 LI:203301.3:2000SEP08 365 577 forward 2 Band_41 FERM domain (Band 4.1 family) 6.30E−16 190 LI:020726.3:2000SEP08 542 1915 forward 2 MCT Monocarboxylate transporter 1.80E−98 191 LI:027209.1:2000SEP08 379 987 forward 1 fibrinogen_C Fibrinogen beta and gamma chains, C- 7.80E−43 terminal globular domain 192 LI:108819.1:2000SEP08 316 828 forward 1 vwa von Willebrand factor type A domain 1.90E−52 193 LI:021759.1:2000SEP08 1136 1246 forward 2 WD40 WD domain, G-beta repeat 1.70E−07 194 LI:1165967.1:2000SEP08 322 462 forward 1 Ribosomal_S27 Ribosomal protein S27a 1.50E−30 194 LI:1165967.1:2000SEP08 22 243 forward 1 ubiquitin Ubiquitin family 4.50E−42 195 LI:1166315.1:2000SEP08 131 283 forward 2 pro_isomerase Cyclophilin type peptidyl-prolyl cis- 1.10E−26 trans isomerase 195 LI:1166315.1:2000SEP08 280 423 forward 1 pro_isomerase Cyclophilin type peptidyl-prolyl cis- 5.50E−17 trans isomerase 195 LI:1166315.1:2000SEP08 423 482 forward 3 pro_isomerase Cyclophilin type peptidyl-prolyl cis- 4.10E−06 trans isomerase 196 LI:204626.1:2000SEP08 322 1212 forward 1 Syntaxin Syntaxin 8.60E−44 197 LI:801140.1:2000SEP08 516 584 forward 3 zf-C2H2 Zinc finger, C2H2 type 2.50E−08 198 LI:286639.1:2000SEP08 1295 1714 forward 2 actin Actin 9.10E−64 198 LI:286639.1:2000SEP08 772 1296 forward 1 actin Actin 1.60E−44 198 LI:286639.1:2000SEP08 630 755 forward 3 actin Actin 1.10E−09 199 LI:288905.4:2000SEP08 285 602 forward 3 CH Calponin homology (CH) domain 5.30E−27 200 LI:332161.1:2000SEP08 75 710 forward 3 ras Ras family 2.00E−48 201 LI:184867.1:2000SEP08 365 478 forward 2 ubiquitin Ubiquitin family 1.40E−04 202 LI:229932.4:2000SEP08 58 969 forward 1 AMP-binding AMP-binding enzyme 3.00E−06 203 LI:1189932.1:2000SEP08 95 1441 forward 2 Folate_carrier Reduced folate carrier 5.80E−10 204 LI:1076689.1:2000SEP08 346 708 forward 1 ribonuclease_T2 Ribonuclease T2 family 6.50E−19 205 LI:415181.2:2000SEP08 505 1584 forward 1 Inos-1-P_synth Myo-inositol-1-phosphate synthase 2.30E−136 205 LI:415181.2:2000SEP08 294 1220 forward 3 Inos-1-P_synth Myo-inositol-1-phosphate synthase 3.40E−16 206 LI:296358.1:2000SEP08 678 1061 forward 3 kinesin Kinesin motor domain 1.40E−46 206 LI:296358.1:2000SEP08 163 510 forward 1 kinesin Kinesin motor domain 6.80E−24 207 LI:205186.3:2000SEP08 476 982 forward 2 lactamase_B Metallo-beta-lactamase superfamily 3.70E−06 208 LI:220537.2:2000SEP08 60 1574 forward 3 sugar_tr Sugar (and other) transporter 6.40E−07 209 LI:248364.2:2000SEP08 253 594 forward 1 BTB BTB/POZ domain 3.60E−04 209 LI:248364.2:2000SEP08 1544 1612 forward 2 zf-C2H2 Zinc finger, C2H2 type 7.10E−06 210 LI:2048338.1:2000SEP08 261 410 forward 3 zf-C3HC4 Zinc finger, C3HC4 type (RING finger) 2.00E−07 211 LI:1185203.8:2000SEP08 333 431 forward 3 ank Ank repeat 2.20E−07 212 LI:021770.3:2000SEP08 287 1171 forward 2 adh_zinc Zinc-binding dehydrogenases 3.70E−08 213 LI:1185841.1:2000SEP08 705 860 forward 3 myosin_head Myosin head (motor domain) 1.80E−07 213 LI:1185841.1:2000SEP08 992 1063 forward 2 myosin_head Myosin head (motor domain) 3.20E−04 214 LI:1181710.1:2000SEP08 62 130 forward 2 zf-C2H2 Zinc finger, C2H2 type 1.10E−05 215 LI:2048959.1:2000SEP08 225 293 forward 3 zf-C2H2 Zinc finger, C2H2 type 4.10E−07 216 LI:798494.1:2000SEP08 273 464 forward 3 KRAB KRAB box 2.00E−42 216 LI:798494.1:2000SEP08 675 743 forward 3 zf-C2H2 Zinc finger, C2H2 type 4.50E−05 216 LI:798494.1:2000SEP08 794 862 forward 2 zf-C2H2 Zinc finger, C2H2 type 6.80E−04 217 LI:2049223.1:2000SEP08 130 318 forward 1 KRAB KRAB box 2.10E−42 218 LI:1177833.1:2000SEP08 78 218 forward 3 KRAB KRAB box 2.30E−17 218 LI:1177833.1:2000SEP08 999 1067 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.70E−04 219 LI:2049267.1:2000SEP08 78 227 forward 3 KRAB KRAB box 3.70E−22 220 LI:1165939.1:2000SEP08 247 315 forward 1 zf-C2H2 Zinc finger, C2H2 type 2.60E−06 221 LI:1170958.1:2000SEP08 397 465 forward 1 zf-C2H2 Zinc finger, C2H2 type 3.20E−07 222 LI:1089827.1:2000SEP08 722 790 forward 2 zf-C2H2 Zinc finger, C2H2 type 3.10E−07 222 LI:1089827.1:2000SEP08 105 173 forward 3 zf-C2H2 Zinc finger, C2H2 type 9.60E−07 222 LI:1089827.1:2000SEP08 433 501 forward 1 zf-C2H2 Zinc finger, C2H2 type 2.10E−06 223 LI:792112.1:2000SEP08 200 268 forward 2 zf-C2H2 Zinc finger, C2H2 type 7.80E−05 224 LI:282219.2:2000SEP08 129 197 forward 3 zf-C2H2 Zinc finger, C2H2 type 4.10E−05 225 LI:1088010.2:2000SEP08 294 362 forward 3 zf-C2H2 Zinc finger, C2H2 type 5.80E−08 226 LI:1165276.1:2000SEP08 195 263 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.80E−06 227 LI:1169524.2:2000SEP08 267 455 forward 3 KRAB KRAB box 2.70E−40 227 LI:1169524.2:2000SEP08 727 795 forward 1 zf-C2H2 Zinc finger, C2H2 type 7.90E−07 228 LI:1180255.1:2000SEP08 440 628 forward 2 KRAB KRAB box 2.30E−33 228 LI:1180255.1:2000SEP08 1027 1095 forward 1 zf-C2H2 Zinc finger, C2H2 type 2.50E−07 229 LI:1091903.1:2000SEP08 182 370 forward 2 KRAB KRAB box 6.20E−39 230 LI:1169219.1:2000SEP08 142 330 forward 1 KRAB KRAB box 3.70E−41 231 LI:2050313.1:2000SEP08 803 982 forward 2 Collagen Collagen triple helix repeat (20 copies) 9.50E−10 232 LI:209351.3:2000SEP08 561 671 forward 3 WD40 WD domain, G-beta repeat 2.20E−06 232 LI:209351.3:2000SEP08 313 423 forward 1 WD40 WD domain, G-beta repeat 1.00E−04 233 LI:119900.1:2000SEP08 179 358 forward 2 KRAB KRAB box 1.50E−34 234 LI:2052274.1:2000SEP08 193 1197 forward 1 A_deaminase Adenosine/AMP deaminase 4.00E−10 235 LI:1075502.1:2000SEP08 100 315 forward 1 OMPdecase Orotidine 5′-phosphate decarboxylase 6.30E−35 235 LI:1075502.1:2000SEP08 305 451 forward 2 OMPdecase Orotidine 5′-phosphate decarboxylase 4.70E−26 235 LI:1075502.1:2000SEP08 426 806 forward 3 OMPdecase Orotidine 5′-phosphate decarboxylase 1.80E−12 236 LI:813697.1:2000SEP08 753 821 forward 3 zf-C2H2 Zinc finger, C2H2 type 1.60E−07 237 LI:814261.1:2000SEP08 3 95 forward 3 GBP Guanylate-binding protein, N-terminal 4.20E−14 domain 238 LI:775334.1:2000SEP08 112 180 forward 1 zf-C2H2 Zinc finger, C2H2 type 2.10E−08 239 LI:1180325.1:2000SEP08 495 563 forward 3 zf-C2H2 Zinc finger, C2H2 type 2.20E−07 240 LI:1183147.3:2000SEP08 82 150 forward 1 zf-C2H2 Zinc finger, C2H2 type 1.20E−04 241 LI:1175373.3:2000SEP08 191 379 forward 2 KRAB KRAB box 6.80E−45 242 LI:813757.1:2000SEP08 268 453 forward 1 KRAB KRAB box 4.30E−38 243 LI:1182979.2:2000SEP08 341 409 forward 2 zf-C2H2 Zinc finger, C2H2 type 3.60E−06 244 LI:1177823.2:2000SEP08 1232 1372 forward 2 KRAB KRAB box 3.00E−15 245 LI:1174279.1:2000SEP08 276 464 forward 3 KRAB KRAB box 1.40E−46 245 LI:1174279.1:2000SEP08 753 821 forward 3 zf-C2H2 Zinc finger, C2H2 type 7.90E−07 246 LI:1178411.1:2000SEP08 787 855 forward 1 zf-C2H2 Zinc finger, C2H2 type 1.20E−07 247 LI:1182739.1:2000SEP08 582 650 forward 3 zf-C2H2 Zinc finger, C2H2 type 6.70E−08 248 LI:234937.4:2000SEP08 61 477 forward 1 DSPc Dual specificity phosphatase, catalytic 8.70E−29 domain 249 LI:1170660.1:2000SEP08 35 103 forward 2 zf-C2H2 Zinc finger, C2H2 type 8.70E−07 250 LI:1144409.1:2000SEP08 16 243 forward 1 pkinase Protein kinase domain 1.30E−10 251 LI:246290.10:2000SEP08 256 453 forward 1 rrm RNA recognition motif. (a.k.a. RRM, 2.10E−08 RBD, or RNP domain) 252 LI:280034.1:2000SEP08 119 652 forward 2 AAA ATPase family associated with various 1.80E−64 cellular activities (AAA)

[0303] TABLE 4 SEQ ID NO: Template ID Start Stop Frame Domain Topology 34 LG:345884.1:2000SEP08 56 142 forward 2 TM N out 35 LG:400967.1:2000SEP08 470 547 forward 2 TM N out 36 LG:024556.6:2000SEP08 529 597 forward 1 TM N in 37 LG:081189.3:2000SEP08 627 686 forward 3 TM N out 38 LG:018258.1:2000SEP08 430 507 forward 1 TM N out 38 LG:018258.1:2000SEP08 444 503 forward 3 TM N out 39 LG:450399.3:2000SEP08 145 231 forward 1 TM N out 39 LG:450399.3:2000SEP08 417 503 forward 3 TM N in 40 LG:451122.1:2000SEP08 328 390 forward 1 TM N in 41 LG:451682.1:2000SEP08 93 155 forward 3 TM 42 LG:238631.4:2000SEP08 526 612 forward 1 TM N out 42 LG:238631.4:2000SEP08 477 563 forward 3 TM 43 LG:236654.1:2000SEP08 236 295 forward 2 TM N out 44 LG:332655.1:2000SEP08 541 621 forward 1 TM N out 44 LG:332655.1:2000SEP08 536 598 forward 2 TM N out 44 LG:332655.1:2000SEP08 626 688 forward 2 TM N out 44 LG:332655.1:2000SEP08 887 949 forward 2 TM N out 44 LG:332655.1:2000SEP08 965 1027 forward 2 TM N out 44 LG:332655.1:2000SEP08 912 998 forward 3 TM N out 45 LG:217396.2:2000SEP08 317 391 forward 2 TM N out 45 LG:217396.2:2000SEP08 1127 1189 forward 2 TM N out 46 LG:090574.1:2000SEP08 49 108 forward 1 TM N out 47 LG:202943.1:2000SEP08 590 658 forward 2 TM N out 47 LG:202943.1:2000SEP08 842 928 forward 2 TM N out 47 LG:202943.1:2000SEP08 552 638 forward 3 TM N out 48 LG:236928.1:2000SEP08 349 435 forward 1 TM N in 48 LG:236928.1:2000SEP08 448 519 forward 1 TM N in 48 LG:236928.1:2000SEP08 592 642 forward 1 TM N in 48 LG:236928.1:2000SEP08 706 768 forward 1 TM N in 48 LG:236928.1:2000SEP08 778 840 forward 1 TM N in 48 LG:236928.1:2000SEP08 967 1038 forward 1 TM N in 48 LG:236928.1:2000SEP08 1318 1374 forward 1 TM N in 48 LG:236928.1:2000SEP08 1609 1695 forward 1 TM N in 48 LG:236928.1:2000SEP08 1933 2016 forward 1 TM N in 48 LG:236928.1:2000SEP08 2161 2247 forward 1 TM N in 48 LG:236928.1:2000SEP08 2419 2475 forward 1 TM N in 48 LG:236928.1:2000SEP08 2818 2865 forward 1 TM N in 48 LG:236928.1:2000SEP08 2884 2946 forward 1 TM N in 48 LG:236928.1:2000SEP08 2980 3042 forward 1 TM N in 48 LG:236928.1:2000SEP08 3076 3138 forward 1 TM N in 48 LG:236928.1:2000SEP08 335 421 forward 2 TM N in 48 LG:236928.1:2000SEP08 437 499 forward 2 TM N in 48 LG:236928.1:2000SEP08 524 586 forward 2 TM N in 48 LG:236928.1:2000SEP08 659 718 forward 2 TM N in 48 LG:236928.1:2000SEP08 1268 1351 forward 2 TM N in 48 LG:236928.1:2000SEP08 1400 1471 forward 2 TM N in 48 LG:236928.1:2000SEP08 1472 1534 forward 2 TM N in 48 LG:236928.1:2000SEP08 1586 1669 forward 2 TM N in 48 LG:236928.1:2000SEP08 1745 1831 forward 2 TM N in 48 LG:236928.1:2000SEP08 1877 1963 forward 2 TM N in 48 LG:236928.1:2000SEP08 2015 2101 forward 2 TM N in 48 LG:236928.1:2000SEP08 2501 2587 forward 2 TM N in 48 LG:236928.1:2000SEP08 2639 2716 forward 2 TM N in 48 LG:236928.1:2000SEP08 2786 2872 forward 2 TM N in 48 LG:236928.1:2000SEP08 2894 2980 forward 2 TM N in 48 LG:236928.1:2000SEP08 471 551 forward 3 TM N in 48 LG:236928.1:2000SEP08 738 824 forward 3 TM N in 48 LG:236928.1:2000SEP08 1287 1340 forward 3 TM N in 48 LG:236928.1:2000SEP08 1626 1712 forward 3 TM N in 48 LG:236928.1:2000SEP08 1890 1976 forward 3 TM N in 48 LG:236928.1:2000SEP08 2034 2120 forward 3 TM N in 48 LG:236928.1:2000SEP08 2118 2186 forward 3 TM N in 48 LG:236928.1:2000SEP08 2520 2591 forward 3 TM N in 48 LG:236928.1:2000SEP08 2763 2846 forward 3 TM N in 48 LG:236928.1:2000SEP08 2916 2978 forward 3 TM N in 48 LG:236928.1:2000SEP08 3003 3065 forward 3 TM N in 49 LG:215169.2:2000SEP08 1363 1413 forward 1 TM N in 49 LG:215169.2:2000SEP08 503 589 forward 2 TM N out 49 LG:215169.2:2000SEP08 1727 1813 forward 2 TM N out 49 LG:215169.2:2000SEP08 237 302 forward 3 TM N out 49 LG:215169.2:2000SEP08 837 923 forward 3 TM N out 49 LG:215169.2:2000SEP08 1398 1460 forward 3 TM N out 49 LG:215169.2:2000SEP08 1470 1532 forward 3 TM N out 49 LG:215169.2:2000SEP08 1605 1658 forward 3 TM N out 50 LG:410726.1:2000SEP08 31 93 forward 1 TM N out 50 LG:410726.1:2000SEP08 115 177 forward 1 TM N out 50 LG:410726.1:2000SEP08 463 549 forward 1 TM N out 51 LG:234372.2:2000SEP08 325 411 forward 1 TM N in 51 LG:234372.2:2000SEP08 2492 2578 forward 2 TM N out 51 LG:234372.2:2000SEP08 2669 2743 forward 2 TM N out 51 LG:234372.2:2000SEP08 723 809 forward 3 TM N in 52 LG:022629.1:2000SEP08 268 354 forward 1 TM N out 52 LG:022629.1:2000SEP08 385 459 forward 1 TM N out 52 LG:022629.1:2000SEP08 559 645 forward 1 TM N out 52 LG:022629.1:2000SEP08 796 882 forward 1 TM N out 52 LG:022629.1:2000SEP08 281 358 forward 2 TM N in 53 LG:068682.1:2000SEP08 707 793 forward 2 TM N out 54 LG:222335.1:2000SEP08 847 933 forward 1 TM N in 54 LG:222335.1:2000SEP08 973 1023 forward 1 TM N in 54 LG:222335.1:2000SEP08 1030 1101 forward 1 TM N in 54 LG:222335.1:2000SEP08 1216 1290 forward 1 TM N in 54 LG:222335.1:2000SEP08 23 109 forward 2 TM 54 LG:222335.1:2000SEP08 314 373 forward 2 TM 54 LG:222335.1:2000SEP08 428 514 forward 2 TM 54 LG:222335.1:2000SEP08 728 784 forward 2 TM 54 LG:222335.1:2000SEP08 794 868 forward 2 TM 54 LG:222335.1:2000SEP08 965 1051 forward 2 TM 54 LG:222335.1:2000SEP08 603 674 forward 3 TM N in 54 LG:222335.1:2000SEP08 921 983 forward 3 TM N in 54 LG:222335.1:2000SEP08 1014 1076 forward 3 TM N in 54 LG:222335.1:2000SEP08 1101 1187 forward 3 TM N in 54 LG:222335.1:2000SEP08 1227 1277 forward 3 TM N in 55 LG:331342.1:2000SEP08 22 96 forward 1 TM N out 55 LG:331342.1:2000SEP08 289 339 forward 1 TM N out 55 LG:331342.1:2000SEP08 645 731 forward 3 TM N in 56 LG:021770.1:2000SEP08 286 372 forward 1 TM N in 56 LG:021770.1:2000SEP08 400 477 forward 1 TM N in 56 LG:021770.1:2000SEP08 502 579 forward 1 TM N in 56 LG:021770.1:2000SEP08 784 852 forward 1 TM N in 56 LG:021770.1:2000SEP08 1237 1323 forward 1 TM N in 56 LG:021770.1:2000SEP08 2416 2499 forward 1 TM N in 56 LG:021770.1:2000SEP08 2611 2697 forward 1 TM N in 56 LG:021770.1:2000SEP08 1115 1201 forward 2 TM N in 56 LG:021770.1:2000SEP08 1262 1336 forward 2 TM N in 56 LG:021770.1:2000SEP08 2426 2509 forward 2 TM N in 56 LG:021770.1:2000SEP08 2726 2776 forward 2 TM N in 56 LG:021770.1:2000SEP08 534 614 forward 3 TM N in 56 LG:021770.1:2000SEP08 1260 1346 forward 3 TM N in 56 LG:021770.1:2000SEP08 1461 1547 forward 3 TM N in 56 LG:021770.1:2000SEP08 1695 1778 forward 3 TM N in 56 LG:021770.1:2000SEP08 2496 2576 forward 3 TM N in 56 LG:021770.1:2000SEP08 2727 2792 forward 3 TM N in 57 LG:181607.9:2000SEP08 439 525 forward 1 TM N out 58 LG:1042768.1:2000SEP08 695 751 forward 2 TM N out 58 LG:1042768.1:2000SEP08 93 143 forward 3 TM N in 58 LG:1042768.1:2000SEP08 201 287 forward 3 TM N in 58 LG:1042768.1:2000SEP08 351 437 forward 3 TM N in 59 LG:282729.1:2000SEP08 256 309 forward 1 TM N out 60 LG:998305.3:2000SEP08 429 488 forward 3 TM N in 60 LG:998305.3:2000SEP08 705 770 forward 3 TM N in 61 LG:1135213.1:2000SEP08 41 127 forward 2 TM N out 61 LG:1135213.1:2000SEP08 215 274 forward 2 TM N out 61 LG:1135213.1:2000SEP08 293 379 forward 2 TM N out 61 LG:1135213.1:2000SEP08 389 475 forward 2 TM N out 62 LG:267762.1:2000SEP08 854 937 forward 2 TM N in 62 LG:267762.1:2000SEP08 1283 1345 forward 2 TM N in 62 LG:267762.1:2000SEP08 1445 1531 forward 2 TM N in 62 LG:267762.1:2000SEP08 1383 1469 forward 3 TM N out 63 LG:120744.1:2000SEP08 181 249 forward 1 TM N out 63 LG:120744.1:2000SEP08 188 256 forward 2 TM 63 LG:120744.1:2000SEP08 275 328 forward 2 TM 64 LG:403409.1:2000SEP08 136 222 forward 1 TM N out 64 LG:403409.1:2000SEP08 973 1029 forward 1 TM N out 64 LG:403409.1:2000SEP08 1285 1371 forward 1 TM N out 64 LG:403409.1:2000SEP08 182 268 forward 2 TM N in 65 LG:226874.3:2000SEP08 231 278 forward 3 TM N out 66 LG:1045521.4:2000SEP08 1216 1266 forward 1 TM N in 66 LG:1045521.4:2000SEP08 1567 1653 forward 1 TM N in 66 LG:1045521.4:2000SEP08 1699 1761 forward 1 TM N in 66 LG:1045521.4:2000SEP08 3091 3177 forward 1 TM N in 66 LG:1045521.4:2000SEP08 3508 3582 forward 1 TM N in 66 LG:1045521.4:2000SEP08 1652 1714 forward 2 TM N in 66 LG:1045521.4:2000SEP08 2444 2500 forward 2 TM N in 66 LG:1045521.4:2000SEP08 2627 2713 forward 2 TM N in 66 LG:1045521.4:2000SEP08 3017 3088 forward 2 TM N in 66 LG:1045521.4:2000SEP08 3317 3385 forward 2 TM N in 66 LG:1045521.4:2000SEP08 1530 1604 forward 3 TM N in 66 LG:1045521.4:2000SEP08 2496 2549 forward 3 TM N in 66 LG:1045521.4:2000SEP08 2931 3017 forward 3 TM N in 66 LG:1045521.4:2000SEP08 3267 3341 forward 3 TM N in 67 LG:275876.1:2000SEP08 775 849 forward 1 TM N in 67 LG:275876.1:2000SEP08 949 1002 forward 1 TM N in 67 LG:275876.1:2000SEP08 842 928 forward 2 TM N out 67 LG:275876.1:2000SEP08 777 842 forward 3 TM N in 68 LG:475127.7:2000SEP08 137 223 forward 2 TM N in 69 LG:157263.1:2000SEP08 175 249 forward 1 TM N in 69 LG:157263.1:2000SEP08 295 345 forward 1 TM N in 69 LG:157263.1:2000SEP08 406 492 forward 1 TM N in 69 LG:157263.1:2000SEP08 793 867 forward 1 TM N in 69 LG:157263.1:2000SEP08 889 951 forward 1 TM N in 69 LG:157263.1:2000SEP08 1081 1143 forward 1 TM N in 69 LG:157263.1:2000SEP08 1168 1230 forward 1 TM N in 69 LG:157263.1:2000SEP08 1255 1341 forward 1 TM N in 69 LG:157263.1:2000SEP08 482 544 forward 2 TM N out 69 LG:157263.1:2000SEP08 563 625 forward 2 TM N out 69 LG:157263.1:2000SEP08 180 266 forward 3 TM N out 70 LG:247382.7:2000SEP08 808 894 forward 1 TM 70 LG:247382.7:2000SEP08 650 709 forward 2 TM N out 70 LG:247382.7:2000SEP08 1412 1495 forward 2 TM N out 71 LG:197367.5:2000SEP08 454 510 forward 1 TM N out 72 LG:218090.5:2000SEP08 85 156 forward 1 TM N out 72 LG:218090.5:2000SEP08 417 494 forward 3 TM N out 73 LG:216612.4:2000SEP08 1615 1701 forward 1 TM N in 73 LG:216612.4:2000SEP08 1942 2007 forward 1 TM N in 73 LG:216612.4:2000SEP08 2182 2268 forward 1 TM N in 73 LG:216612.4:2000SEP08 2413 2487 forward 1 TM N in 73 LG:216612.4:2000SEP08 1583 1660 forward 2 TM N in 73 LG:216612.4:2000SEP08 2114 2176 forward 2 TM N in 73 LG:216612.4:2000SEP08 2216 2278 forward 2 TM N in 73 LG:216612.4:2000SEP08 2339 2425 forward 2 TM N in 73 LG:216612.4:2000SEP08 2483 2542 forward 2 TM N in 73 LG:216612.4:2000SEP08 120 206 forward 3 TM N in 73 LG:216612.4:2000SEP08 234 284 forward 3 TM N in 73 LG:216612.4:2000SEP08 327 413 forward 3 TM N in 73 LG:216612.4:2000SEP08 444 530 forward 3 TM N in 73 LG:216612.4:2000SEP08 810 896 forward 3 TM N in 73 LG:216612.4:2000SEP08 942 1028 forward 3 TM N in 73 LG:216612.4:2000SEP08 1644 1730 forward 3 TM N in 73 LG:216612.4:2000SEP08 1950 2012 forward 3 TM N in 73 LG:216612.4:2000SEP08 2037 2099 forward 3 TM N in 73 LG:216612.4:2000SEP08 2292 2378 forward 3 TM N in 73 LG:216612.4:2000SEP08 2529 2615 forward 3 TM N in 74 LG:197614.1:2000SEP08 484 537 forward 1 TM N in 74 LG:197614.1:2000SEP08 2308 2367 forward 1 TM N in 74 LG:197614.1:2000SEP08 3175 3246 forward 1 TM N in 74 LG:197614.1:2000SEP08 3298 3354 forward 1 TM N in 74 LG:197614.1:2000SEP08 3556 3612 forward 1 TM N in 74 LG:197614.1:2000SEP08 3739 3825 forward 1 TM N in 74 LG:197614.1:2000SEP08 3964 4050 forward 1 TM N in 74 LG:197614.1:2000SEP08 4063 4134 forward 1 TM N in 74 LG:197614.1:2000SEP08 4147 4215 forward 1 TM N in 74 LG:197614.1:2000SEP08 374 460 forward 2 TM N out 74 LG:197614.1:2000SEP08 800 862 forward 2 TM N out 74 LG:197614.1:2000SEP08 875 937 forward 2 TM N out 74 LG:197614.1:2000SEP08 1352 1414 forward 2 TM N out 74 LG:197614.1:2000SEP08 1436 1498 forward 2 TM N out 74 LG:197614.1:2000SEP08 2312 2398 forward 2 TM N out 74 LG:197614.1:2000SEP08 3422 3469 forward 2 TM N out 74 LG:197614.1:2000SEP08 3632 3718 forward 2 TM N out 74 LG:197614.1:2000SEP08 3773 3835 forward 2 TM N out 74 LG:197614.1:2000SEP08 3932 4003 forward 2 TM N out 74 LG:197614.1:2000SEP08 4040 4126 forward 2 TM N out 74 LG:197614.1:2000SEP08 4244 4312 forward 2 TM N out 74 LG:197614.1:2000SEP08 4448 4504 forward 2 TM N out 74 LG:197614.1:2000SEP08 489 575 forward 3 TM 74 LG:197614.1:2000SEP08 2967 3017 forward 3 TM 74 LG:197614.1:2000SEP08 3663 3749 forward 3 TM 74 LG:197614.1:2000SEP08 3912 3974 forward 3 TM 74 LG:197614.1:2000SEP08 4020 4082 forward 3 TM 74 LG:197614.1:2000SEP08 4341 4427 forward 3 TM 75 LG:378428.1:2000SEP08 703 789 forward 1 TM N in 75 LG:378428.1:2000SEP08 1336 1422 forward 1 TM N in 75 LG:378428.1:2000SEP08 1924 2010 forward 1 TM N in 75 LG:378428.1:2000SEP08 2188 2268 forward 1 TM N in 75 LG:378428.1:2000SEP08 2171 2224 forward 2 TM N in 75 LG:378428.1:2000SEP08 1527 1577 forward 3 TM N out 75 LG:378428.1:2000SEP08 1665 1751 forward 3 TM N out 75 LG:378428.1:2000SEP08 1968 2054 forward 3 TM N out 75 LG:378428.1:2000SEP08 2205 2291 forward 3 TM N out 76 LG:286639.1:2000SEP08 127 213 forward 1 TM 76 LG:286639.1:2000SEP08 970 1032 forward 1 TM 76 LG:286639.1:2000SEP08 1066 1128 forward 1 TM 76 LG:286639.1:2000SEP08 1588 1662 forward 1 TM 76 LG:286639.1:2000SEP08 1786 1872 forward 1 TM 76 LG:286639.1:2000SEP08 62 148 forward 2 TM N in 76 LG:286639.1:2000SEP08 1772 1825 forward 2 TM N in 76 LG:286639.1:2000SEP08 267 320 forward 3 TM N out 76 LG:286639.1:2000SEP08 999 1085 forward 3 TM N out 76 LG:286639.1:2000SEP08 1902 1967 forward 3 TM N out 77 LG:389870.1:2000SEP08 1066 1113 forward 1 TM N out 77 LG:389870.1:2000SEP08 1055 1120 forward 2 TM N in 77 LG:389870.1:2000SEP08 1059 1142 forward 3 TM N in 78 LG:1387485.6:2000SEP08 1213 1275 forward 1 TM N in 78 LG:1387485.6:2000SEP08 206 292 forward 2 TM N in 78 LG:1387485.6:2000SEP08 824 886 forward 2 TM N in 78 LG:1387485.6:2000SEP08 914 976 forward 2 TM N in 78 LG:1387485.6:2000SEP08 1244 1321 forward 2 TM N in 78 LG:1387485.6:2000SEP08 396 473 forward 3 TM N out 78 LG:1387485.6:2000SEP08 537 602 forward 3 TM N out 78 LG:1387485.6:2000SEP08 660 746 forward 3 TM N out 78 LG:1387485.6:2000SEP08 786 872 forward 3 TM N out 78 LG:1387485.6:2000SEP08 1164 1226 forward 3 TM N out 78 LG:1387485.6:2000SEP08 1245 1307 forward 3 TM N out 79 LG:230151.1:2000SEP08 1774 1860 forward 1 TM N in 79 LG:230151.1:2000SEP08 1091 1165 forward 2 TM N out 79 LG:230151.1:2000SEP08 1193 1246 forward 2 TM N out 79 LG:230151.1:2000SEP08 1757 1843 forward 2 TM N out 80 LG:215158.5:2000SEP08 199 267 forward 1 TM N out 80 LG:215158.5:2000SEP08 820 873 forward 1 TM N out 80 LG:215158.5:2000SEP08 892 945 forward 1 TM N out 80 LG:215158.5:2000SEP08 908 985 forward 2 TM N out 80 LG:215158.5:2000SEP08 1433 1504 forward 2 TM N out 80 LG:215158.5:2000SEP08 447 533 forward 3 TM 81 LG:235840.1:2000SEP08 265 342 forward 1 TM N out 81 LG:235840.1:2000SEP08 511 579 forward 1 TM N out 81 LG:235840.1:2000SEP08 577 639 forward 1 TM N out 81 LG:235840.1:2000SEP08 730 786 forward 1 TM N out 81 LG:235840.1:2000SEP08 2011 2082 forward 1 TM N out 81 LG:235840.1:2000SEP08 2110 2172 forward 1 TM N out 81 LG:235840.1:2000SEP08 2326 2406 forward 1 TM N out 81 LG:235840.1:2000SEP08 2416 2502 forward 1 TM N out 81 LG:235840.1:2000SEP08 116 178 forward 2 TM N out 81 LG:235840.1:2000SEP08 191 253 forward 2 TM N out 81 LG:235840.1:2000SEP08 500 586 forward 2 TM N out 81 LG:235840.1:2000SEP08 731 817 forward 2 TM N out 81 LG:235840.1:2000SEP08 848 916 forward 2 TM N out 81 LG:235840.1:2000SEP08 956 1030 forward 2 TM N out 81 LG:235840.1:2000SEP08 1973 2050 forward 2 TM N out 81 LG:235840.1:2000SEP08 192 278 forward 3 TM N out 81 LG:235840.1:2000SEP08 516 590 forward 3 TM N out 81 LG:235840.1:2000SEP08 711 797 forward 3 TM N out 81 LG:235840.1:2000SEP08 819 905 forward 3 TM N out 81 LG:235840.1:2000SEP08 1446 1529 forward 3 TM N out 81 LG:235840.1:2000SEP08 1893 1976 forward 3 TM N out 81 LG:235840.1:2000SEP08 2298 2360 forward 3 TM N out 82 LG:350272.1:2000SEP08 1675 1746 forward 1 TM N in 82 LG:350272.1:2000SEP08 2374 2436 forward 1 TM N in 82 LG:350272.1:2000SEP08 104 190 forward 2 TM N in 82 LG:350272.1:2000SEP08 2264 2332 forward 2 TM N in 82 LG:350272.1:2000SEP08 2369 2440 forward 2 TM N in 82 LG:350272.1:2000SEP08 12 95 forward 3 TM N in 82 LG:350272.1:2000SEP08 993 1052 forward 3 TM N in 82 LG:350272.1:2000SEP08 2067 2138 forward 3 TM N in 82 LG:350272.1:2000SEP08 2334 2399 forward 3 TM N in 83 LG:232190.1:2000SEP08 592 678 forward 1 TM N in 83 LG:232190.1:2000SEP08 1423 1500 forward 1 TM N in 83 LG:232190.1:2000SEP08 158 241 forward 2 TM N in 83 LG:232190.1:2000SEP08 293 373 forward 2 TM N in 83 LG:232190.1:2000SEP08 644 730 forward 2 TM N in 83 LG:232190.1:2000SEP08 761 847 forward 2 TM N in 83 LG:232190.1:2000SEP08 1466 1552 forward 2 TM N in 83 LG:232190.1:2000SEP08 279 356 forward 3 TM N in 83 LG:232190.1:2000SEP08 588 674 forward 3 TM N in 83 LG:232190.1:2000SEP08 936 1022 forward 3 TM N in 84 LG:1068127.1:2000SEP08 423 470 forward 3 TM 85 LG:408751.3:2000SEP08 2194 2253 forward 1 TM N out 85 LG:408751.3:2000SEP08 2320 2406 forward 1 TM N out 85 LG:408751.3:2000SEP08 1907 1993 forward 2 TM N out 85 LG:408751.3:2000SEP08 2378 2464 forward 2 TM N out 85 LG:408751.3:2000SEP08 1866 1928 forward 3 TM N in 85 LG:408751.3:2000SEP08 2328 2414 forward 3 TM N in 86 LG:1078933.1:2000SEP08 905 991 forward 2 TM N in 86 LG:1078933.1:2000SEP08 924 1010 forward 3 TM N in 87 LG:958731.1:2000SEP08 15 101 forward 3 TM N out 88 LG:024125.5:2000SEP08 474 554 forward 3 TM 89 LG:373637.3:2000SEP08 473 559 forward 2 TM N in 89 LG:373637.3:2000SEP08 854 934 forward 2 TM N in 90 LG:1053229.1:2000SEP08 410 487 forward 2 TM N out 91 LG:248364.1:2000SEP08 439 495 forward 1 TM N out 92 LG:477130.1:2000SEP08 37 108 forward 1 TM N in 92 LG:477130.1:2000SEP08 406 489 forward 1 TM N in 92 LG:477130.1:2000SEP08 685 759 forward 1 TM N in 92 LG:477130.1:2000SEP08 641 727 forward 2 TM N in 92 LG:477130.1:2000SEP08 741 827 forward 3 TM N in 93 LG:113786.17:2000SEP08 89 139 forward 2 TM N out 93 LG:113786.17:2000SEP08 18 68 forward 3 TM 94 LG:347635.1:2000SEP08 220 294 forward 1 TM N out 94 LG:347635.1:2000SEP08 406 456 forward 1 TM N out 94 LG:347635.1:2000SEP08 479 550 forward 2 TM N out 94 LG:347635.1:2000SEP08 1283 1369 forward 2 TM N out 94 LG:347635.1:2000SEP08 615 701 forward 3 TM N out 94 LG:347635.1:2000SEP08 1347 1397 forward 3 TM N out 95 LG:242966.4:2000SEP08 1439 1510 forward 2 TM N in 96 LG:217814.1:2000SEP08 1621 1689 forward 1 TM N out 96 LG:217814.1:2000SEP08 1622 1708 forward 2 TM N out 96 LG:217814.1:2000SEP08 246 302 forward 3 TM N in 96 LG:217814.1:2000SEP08 1695 1772 forward 3 TM N in 97 LG:476452.1:2000SEP08 556 624 forward 1 TM N out 97 LG:476452.1:2000SEP08 988 1074 forward 1 TM N out 98 LG:1100657.1:2000SEP08 31 117 forward 1 TM N out 99 LG:1132418.2:2000SEP08 43 129 forward 1 TM N out 99 LG:1132418.2:2000SEP08 244 327 forward 1 TM N out 100 LG:1098570.1:2000SEP08 400 453 forward 1 TM N out 100 LG:1098570.1:2000SEP08 26 85 forward 2 TM N out 101 LG:1097987.1:2000SEP08 152 208 forward 2 TM N out 101 LG:1097987.1:2000SEP08 141 215 forward 3 TM 101 LG:1097987.1:2000SEP08 912 971 forward 3 TM 102 LG:337818.2:2000SEP08 40 117 forward 1 TM N out 102 LG:337818.2:2000SEP08 532 618 forward 1 TM N out 102 LG:337818.2:2000SEP08 907 993 forward 1 TM N out 102 LG:337818.2:2000SEP08 1360 1425 forward 1 TM N out 103 LG:1040582.1:2000SEP08 31 117 forward 1 TM N in 103 LG:1040582.1:2000SEP08 539 595 forward 2 TM N out 103 LG:1040582.1:2000SEP08 330 416 forward 3 TM N out 104 LG:1099122.1:2000SEP08 385 456 forward 1 TM N out 104 LG:1099122.1:2000SEP08 236 292 forward 2 TM N in 104 LG:1099122.1:2000SEP08 350 436 forward 2 TM N in 104 LG:1099122.1:2000SEP08 258 308 forward 3 TM N out 104 LG:1099122.1:2000SEP08 420 470 forward 3 TM N out 105 LG:1327449.1:2000SEP08 112 198 forward 1 TM N out 105 LG:1327449.1:2000SEP08 268 318 forward 1 TM N out 105 LG:1327449.1:2000SEP08 395 481 forward 2 TM N out 106 LG:227933.5:2000SEP08 1114 1200 forward 1 TM N in 106 LG:227933.5:2000SEP08 1231 1290 forward 1 TM N in 106 LG:227933.5:2000SEP08 255 308 forward 3 TM N out 107 LG:1043709.2:2000SEP08 600 650 forward 3 TM N out 108 LG:1099871.1:2000SEP08 181 243 forward 1 TM N out 109 LG:1399139.4:2000SEP08 289 369 forward 1 TM N out 109 LG:1399139.4:2000SEP08 616 684 forward 1 TM N out 109 LG:1399139.4:2000SEP08 185 235 forward 2 TM 109 LG:1399139.4:2000SEP08 555 641 forward 3 TM N out 110 LG:236386.1:2000SEP08 106 171 forward 1 TM N out 110 LG:236386.1:2000SEP08 271 357 forward 1 TM N out 110 LG:236386.1:2000SEP08 3097 3159 forward 1 TM N out 110 LG:236386.1:2000SEP08 3715 3789 forward 1 TM N out 110 LG:236386.1:2000SEP08 3093 3164 forward 3 TM N out 110 LG:236386.1:2000SEP08 3759 3812 forward 3 TM N out 111 LG:1015157.1:2000SEP08 320 406 forward 2 TM N in 112 LG:1065433.1:2000SEP08 790 876 forward 1 TM N in 113 LG:236992.4:2000SEP08 421 471 forward 1 TM N out 113 LG:236992.4:2000SEP08 14 100 forward 2 TM N out 114 LG:1071124.1:2000SEP08 171 257 forward 3 TM N out 115 LG:206425.2:2000SEP08 175 237 forward 1 TM N in 115 LG:206425.2:2000SEP08 424 483 forward 1 TM N in 115 LG:206425.2:2000SEP08 1810 1896 forward 1 TM N in 115 LG:206425.2:2000SEP08 1939 2001 forward 1 TM N in 115 LG:206425.2:2000SEP08 404 457 forward 2 TM N in 115 LG:206425.2:2000SEP08 2168 2254 forward 2 TM N in 115 LG:206425.2:2000SEP08 561 620 forward 3 TM N out 115 LG:206425.2:2000SEP08 1908 1994 forward 3 TM N out 116 LG:885747.2:2000SEP08 125 205 forward 2 TM N in 116 LG:885747.2:2000SEP08 135 191 forward 3 TM N out 116 LG:885747.2:2000SEP08 189 239 forward 3 TM N out 117 LG:1140501.1:2000SEP08 622 708 forward 1 TM N out 117 LG:1140501.1:2000SEP08 844 918 forward 1 TM N out 117 LG:1140501.1:2000SEP08 1138 1206 forward 1 TM N out 117 LG:1140501.1:2000SEP08 86 169 forward 2 TM N out 117 LG:1140501.1:2000SEP08 221 301 forward 2 TM N out 117 LG:1140501.1:2000SEP08 617 703 forward 2 TM N out 117 LG:1140501.1:2000SEP08 606 677 forward 3 TM N in 118 LG:001239.1:2000SEP08 1048 1122 forward 1 TM N out 118 LG:001239.1:2000SEP08 669 755 forward 3 TM N out 118 LG:001239.1:2000SEP08 1911 1976 forward 3 TM N out 119 LG:018980.1:2000SEP08 124 204 forward 1 TM N out 119 LG:018980.1:2000SEP08 944 997 forward 2 TM N out 119 LG:018980.1:2000SEP08 405 464 forward 3 TM N out 119 LG:018980.1:2000SEP08 900 986 forward 3 TM N out 119 LG:018980.1:2000SEP08 1017 1103 forward 3 TM N out 120 LG:1083120.3:2000SEP08 214 291 forward 1 TM N out 120 LG:1083120.3:2000SEP08 233 319 forward 2 TM N out 120 LG:1083120.3:2000SEP08 252 320 forward 3 TM N in 121 LG:233258.3:2000SEP08 58 141 forward 1 TM 121 LG:233258.3:2000SEP08 1783 1842 forward 1 TM 121 LG:233258.3:2000SEP08 2248 2322 forward 1 TM 121 LG:233258.3:2000SEP08 4522 4596 forward 1 TM 121 LG:233258.3:2000SEP08 4208 4294 forward 2 TM N out 121 LG:233258.3:2000SEP08 4478 4534 forward 2 TM N out 121 LG:233258.3:2000SEP08 390 476 forward 3 TM N in 121 LG:233258.3:2000SEP08 2766 2852 forward 3 TM N in 122 LG:999062.1:2000SEP08 455 508 forward 2 TM N in 122 LG:999062.1:2000SEP08 510 596 forward 3 TM N in 123 LG:887776.1:2000SEP08 14 91 forward 2 TM N out 124 LG:1400301.2:2000SEP08 445 531 forward 1 TM N out 124 LG:1400301.2:2000SEP08 456 518 forward 3 TM N out 125 LG:1329362.1:2000SEP08 18 104 forward 3 TM N out 126 LG:1096498.1:2000SEP08 137 199 forward 2 TM N out 126 LG:1096498.1:2000SEP08 201 269 forward 3 TM N out 126 LG:1096498.1:2000SEP08 321 371 forward 3 TM N out 127 LG:1096337.1:2000SEP08 625 711 forward 1 TM N out 127 LG:1096337.1:2000SEP08 500 553 forward 2 TM 128 LG:1400579.1:2000SEP08 797 883 forward 2 TM N out 128 LG:1400579.1:2000SEP08 9 86 forward 3 TM N out 128 LG:1400579.1:2000SEP08 669 755 forward 3 TM N out 129 LG:1080091.1:2000SEP08 67 114 forward 1 TM N out 129 LG:1080091.1:2000SEP08 435 497 forward 3 TM N out 130 LG:1082203.1:2000SEP08 1438 1521 forward 1 TM N in 130 LG:1082203.1:2000SEP08 155 217 forward 2 TM N out 130 LG:1082203.1:2000SEP08 272 358 forward 2 TM N out 131 LG:1084051.1:2000SEP08 301 366 forward 1 TM N out 131 LG:1084051.1:2000SEP08 934 1017 forward 1 TM N out 131 LG:1084051.1:2000SEP08 1072 1140 forward 1 TM N out 131 LG:1084051.1:2000SEP08 875 961 forward 2 TM N out 131 LG:1084051.1:2000SEP08 882 968 forward 3 TM N in 131 LG:1084051.1:2000SEP08 1071 1151 forward 3 TM N in 132 LG:1082393.1:2000SEP08 505 579 forward 1 TM N in 132 LG:1082393.1:2000SEP08 1710 1784 forward 3 TM N in 133 LG:1086183.1:2000SEP08 1093 1179 forward 1 TM N out 133 LG:1086183.1:2000SEP08 1166 1252 forward 2 TM N in 133 LG:1086183.1:2000SEP08 15 86 forward 3 TM 133 LG:1086183.1:2000SEP08 381 437 forward 3 TM 133 LG:1086183.1:2000SEP08 1194 1280 forward 3 TM 134 LG:1090268.1:2000SEP08 1882 1953 forward 1 TM N out 134 LG:1090268.1:2000SEP08 1969 2055 forward 1 TM N out 134 LG:1090268.1:2000SEP08 1670 1729 forward 2 TM N out 134 LG:1090268.1:2000SEP08 1853 1939 forward 2 TM N out 134 LG:1090268.1:2000SEP08 1997 2083 forward 2 TM N out 134 LG:1090268.1:2000SEP08 1485 1550 forward 3 TM N in 134 LG:1090268.1:2000SEP08 1869 1943 forward 3 TM N in 134 LG:1090268.1:2000SEP08 1962 2048 forward 3 TM N in 135 LG:1400597.5:2000SEP08 134 199 forward 2 TM N in 136 LG:1080307.2:2000SEP08 275 346 forward 2 TM N out 136 LG:1080307.2:2000SEP08 347 403 forward 2 TM N out 136 LG:1080307.2:2000SEP08 183 269 forward 3 TM N in 136 LG:1080307.2:2000SEP08 303 371 forward 3 TM N in 137 LG:1400603.2:2000SEP08 792 878 forward 3 TM N in 137 LG:1400603.2:2000SEP08 903 971 forward 3 TM N in 137 LG:1400603.2:2000SEP08 1068 1151 forward 3 TM N in 138 LG:1052984.1:2000SEP08 496 582 forward 1 TM N in 138 LG:1052984.1:2000SEP08 509 595 forward 2 TM N out 138 LG:1052984.1:2000SEP08 495 581 forward 3 TM 139 LG:1091259.1:2000SEP08 799 885 forward 1 TM N in 140 LG:1082263.2:2000SEP08 1390 1458 forward 1 TM N in 140 LG:1082263.2:2000SEP08 1558 1644 forward 1 TM N in 140 LG:1082263.2:2000SEP08 83 169 forward 2 TM 140 LG:1082263.2:2000SEP08 1526 1612 forward 2 TM 140 LG:1082263.2:2000SEP08 1578 1664 forward 3 TM N in 141 LG:1048604.2:2000SEP08 562 618 forward 1 TM N in 141 LG:1048604.2:2000SEP08 697 768 forward 1 TM N in 141 LG:1048604.2:2000SEP08 856 930 forward 1 TM N in 141 LG:1048604.2:2000SEP08 332 418 forward 2 TM N in 141 LG:1048604.2:2000SEP08 689 775 forward 2 TM N in 141 LG:1048604.2:2000SEP08 1115 1192 forward 2 TM N in 141 LG:1048604.2:2000SEP08 483 557 forward 3 TM N in 141 LG:1048604.2:2000SEP08 570 638 forward 3 TM N in 141 LG:1048604.2:2000SEP08 678 743 forward 3 TM N in 141 LG:1048604.2:2000SEP08 1113 1199 forward 3 TM N in 142 LG:1085254.3:2000SEP08 331 378 forward 1 TM N in 142 LG:1085254.3:2000SEP08 204 290 forward 3 TM N out 143 LG:1400606.2:2000SEP08 1096 1176 forward 1 TM N out 143 LG:1400606.2:2000SEP08 794 880 forward 2 TM N in 143 LG:1400606.2:2000SEP08 1031 1117 forward 2 TM N in 143 LG:1400606.2:2000SEP08 93 173 forward 3 TM N in 143 LG:1400606.2:2000SEP08 765 851 forward 3 TM N in 144 LG:1090358.2:2000SEP08 250 336 forward 1 TM N in 144 LG:1090358.2:2000SEP08 758 844 forward 2 TM N out 144 LG:1090358.2:2000SEP08 848 919 forward 2 TM N out 144 LG:1090358.2:2000SEP08 974 1060 forward 2 TM N out 145 LG:1079064.2:2000SEP08 862 936 forward 1 TM N out 146 LG:1076866.1:2000SEP08 2113 2187 forward 1 TM N in 146 LG:1076866.1:2000SEP08 2111 2170 forward 2 TM 146 LG:1076866.1:2000SEP08 501 587 forward 3 TM N in 146 LG:1076866.1:2000SEP08 2148 2234 forward 3 TM N in 147 LG:969359.1:2000SEP08 256 303 forward 1 TM N out 147 LG:969359.1:2000SEP08 276 350 forward 3 TM N out 148 LG:366783.1:2000SEP08 1060 1143 forward 1 TM N in 148 LG:366783.1:2000SEP08 470 550 forward 2 TM 148 LG:366783.1:2000SEP08 1050 1109 forward 3 TM N in 149 LG:332176.3:2000SEP08 442 495 forward 1 TM N in 149 LG:332176.3:2000SEP08 209 295 forward 2 TM N in 149 LG:332176.3:2000SEP08 234 299 forward 3 TM N in 149 LG:332176.3:2000SEP08 792 851 forward 3 TM N in 149 LG:332176.3:2000SEP08 876 938 forward 3 TM N in 149 LG:332176.3:2000SEP08 966 1028 forward 3 TM N in 150 LG:994938.1:2000SEP08 562 618 forward 1 TM N out 150 LG:994938.1:2000SEP08 287 343 forward 2 TM N out 150 LG:994938.1:2000SEP08 512 598 forward 2 TM N out 150 LG:994938.1:2000SEP08 279 356 forward 3 TM N out 150 LG:994938.1:2000SEP08 474 557 forward 3 TM N out 151 LG:982800.1:2000SEP08 25 81 forward 1 TM N out 151 LG:982800.1:2000SEP08 1708 1782 forward 1 TM N out 151 LG:982800.1:2000SEP08 2305 2391 forward 1 TM N out 151 LG:982800.1:2000SEP08 1658 1744 forward 2 TM N in 151 LG:982800.1:2000SEP08 1880 1927 forward 2 TM N in 151 LG:982800.1:2000SEP08 2255 2341 forward 2 TM N in 151 LG:982800.1:2000SEP08 1614 1697 forward 3 TM N in 151 LG:982800.1:2000SEP08 2220 2306 forward 3 TM N in 152 LG:977850.7:2000SEP08 58 144 forward 1 TM N out 152 LG:977850.7:2000SEP08 187 237 forward 1 TM N out 152 LG:977850.7:2000SEP08 35 112 forward 2 TM N out 152 LG:977850.7:2000SEP08 48 116 forward 3 TM N in 153 LG:234748.2:2000SEP08 25 99 forward 1 TM N out 153 LG:234748.2:2000SEP08 601 663 forward 1 TM N out 153 LG:234748.2:2000SEP08 679 741 forward 1 TM N out 153 LG:234748.2:2000SEP08 871 957 forward 1 TM N out 153 LG:234748.2:2000SEP08 1162 1230 forward 1 TM N out 153 LG:234748.2:2000SEP08 1237 1302 forward 1 TM N out 153 LG:234748.2:2000SEP08 1579 1641 forward 1 TM N out 153 LG:234748.2:2000SEP08 1984 2070 forward 1 TM N out 153 LG:234748.2:2000SEP08 2110 2196 forward 1 TM N out 153 LG:234748.2:2000SEP08 2308 2355 forward 1 TM N out 153 LG:234748.2:2000SEP08 359 421 forward 2 TM 153 LG:234748.2:2000SEP08 464 526 forward 2 TM 153 LG:234748.2:2000SEP08 656 742 forward 2 TM 153 LG:234748.2:2000SEP08 899 949 forward 2 TM 153 LG:234748.2:2000SEP08 995 1057 forward 2 TM 153 LG:234748.2:2000SEP08 1076 1138 forward 2 TM 153 LG:234748.2:2000SEP08 1412 1489 forward 2 TM 153 LG:234748.2:2000SEP08 1925 1999 forward 2 TM 153 LG:234748.2:2000SEP08 2012 2071 forward 2 TM 153 LG:234748.2:2000SEP08 2105 2191 forward 2 TM 153 LG:234748.2:2000SEP08 2204 2290 forward 2 TM 153 LG:234748.2:2000SEP08 393 455 forward 3 TM N in 153 LG:234748.2:2000SEP08 474 536 forward 3 TM N in 153 LG:234748.2:2000SEP08 645 725 forward 3 TM N in 153 LG:234748.2:2000SEP08 801 863 forward 3 TM N in 153 LG:234748.2:2000SEP08 894 956 forward 3 TM N in 153 LG:234748.2:2000SEP08 1485 1535 forward 3 TM N in 153 LG:234748.2:2000SEP08 2052 2114 forward 3 TM N in 153 LG:234748.2:2000SEP08 2145 2207 forward 3 TM N in 153 LG:234748.2:2000SEP08 2238 2300 forward 3 TM N in 154 LG:306284.1:2000SEP08 255 305 forward 3 TM N in 177 LI:335923.2:2000SEP08 149 229 forward 2 TM N in 178 LI:345884.1:2000SEP08 61 147 forward 1 TM N out 179 LI:417127.1:2000SEP08 148 201 forward 1 TM N in 179 LI:417127.1:2000SEP08 114 200 forward 3 TM N in 180 LI:451710.1:2000SEP08 502 588 forward 1 TM N in 180 LI:451710.1:2000SEP08 453 515 forward 3 TM N in 181 LI:406882.2:2000SEP08 109 180 forward 1 TM N in 181 LI:406882.2:2000SEP08 514 597 forward 1 TM N in 181 LI:406882.2:2000SEP08 1045 1101 forward 1 TM N in 181 LI:406882.2:2000SEP08 293 379 forward 2 TM N out 181 LI:406882.2:2000SEP08 653 739 forward 2 TM N out 181 LI:406882.2:2000SEP08 1091 1141 forward 2 TM N out 181 LI:406882.2:2000SEP08 675 746 forward 3 TM N out 182 LI:728223.1:2000SEP08 45 131 forward 3 TM N out 182 LI:728223.1:2000SEP08 129 179 forward 3 TM N out 183 LI:289783.19:2000SEP08 10 93 forward 1 TM N in 183 LI:289783.19:2000SEP08 151 204 forward 1 TM N in 183 LI:289783.19:2000SEP08 11 94 forward 2 TM 183 LI:289783.19:2000SEP08 140 226 forward 2 TM 183 LI:289783.19:2000SEP08 489 575 forward 3 TM N in 184 LI:235255.8:2000SEP08 985 1044 forward 1 TM N out 185 LI:237693.5:2000SEP08 355 429 forward 1 TM N in 186 LI:433670.3:2000SEP08 79 165 forward 1 TM 186 LI:433670.3:2000SEP08 598 681 forward 1 TM 186 LI:433670.3:2000SEP08 796 867 forward 1 TM 186 LI:433670.3:2000SEP08 74 160 forward 2 TM N in 186 LI:433670.3:2000SEP08 221 292 forward 2 TM N in 186 LI:433670.3:2000SEP08 662 736 forward 2 TM N in 186 LI:433670.3:2000SEP08 848 898 forward 2 TM N in 186 LI:433670.3:2000SEP08 75 161 forward 3 TM N in 186 LI:433670.3:2000SEP08 387 449 forward 3 TM N in 186 LI:433670.3:2000SEP08 651 737 forward 3 TM N in 187 LI:202943.4:2000SEP08 535 609 forward 1 TM N out 187 LI:202943.4:2000SEP08 1570 1656 forward 1 TM N out 187 LI:202943.4:2000SEP08 342 395 forward 3 TM N out 187 LI:202943.4:2000SEP08 495 557 forward 3 TM N out 187 LI:202943.4:2000SEP08 579 641 forward 3 TM N out 187 LI:202943.4:2000SEP08 759 845 forward 3 TM N out 187 LI:202943.4:2000SEP08 1653 1721 forward 3 TM N out 187 LI:202943.4:2000SEP08 1905 1991 forward 3 TM N out 188 LI:068682.1:2000SEP08 700 786 forward 1 TM N out 189 LI:203301.3:2000SEP08 643 729 forward 1 TM N out 189 LI:203301.3:2000SEP08 1510 1572 forward 1 TM N out 189 LI:203301.3:2000SEP08 1585 1647 forward 1 TM N out 189 LI:203301.3:2000SEP08 1774 1842 forward 1 TM N out 189 LI:203301.3:2000SEP08 2014 2100 forward 1 TM N out 189 LI:203301.3:2000SEP08 2158 2220 forward 1 TM N out 189 LI:203301.3:2000SEP08 2383 2469 forward 1 TM N out 189 LI:203301.3:2000SEP08 2548 2634 forward 1 TM N out 189 LI:203301.3:2000SEP08 2662 2724 forward 1 TM N out 189 LI:203301.3:2000SEP08 2749 2835 forward 1 TM N out 189 LI:203301.3:2000SEP08 1685 1771 forward 2 TM N in 189 LI:203301.3:2000SEP08 2162 2233 forward 2 TM N in 189 LI:203301.3:2000SEP08 2342 2428 forward 2 TM N in 189 LI:203301.3:2000SEP08 2519 2572 forward 2 TM N in 189 LI:203301.3:2000SEP08 2597 2674 forward 2 TM N in 189 LI:203301.3:2000SEP08 117 170 forward 3 TM N in 189 LI:203301.3:2000SEP08 387 470 forward 3 TM N in 189 LI:203301.3:2000SEP08 1086 1136 forward 3 TM N in 189 LI:203301.3:2000SEP08 1344 1430 forward 3 TM N in 189 LI:203301.3:2000SEP08 1626 1712 forward 3 TM N in 189 LI:203301.3:2000SEP08 2364 2435 forward 3 TM N in 189 LI:203301.3:2000SEP08 2604 2672 forward 3 TM N in 190 LI:020726.3:2000SEP08 1363 1449 forward 1 TM N in 190 LI:020726.3:2000SEP08 1795 1863 forward 1 TM N in 190 LI:020726.3:2000SEP08 1930 1992 forward 1 TM N in 190 LI:020726.3:2000SEP08 545 631 forward 2 TM N in 190 LI:020726.3:2000SEP08 656 742 forward 2 TM N in 190 LI:020726.3:2000SEP08 767 829 forward 2 TM N in 190 LI:020726.3:2000SEP08 839 901 forward 2 TM N in 190 LI:020726.3:2000SEP08 938 1024 forward 2 TM N in 190 LI:020726.3:2000SEP08 1391 1477 forward 2 TM N in 190 LI:020726.3:2000SEP08 1598 1672 forward 2 TM N in 190 LI:020726.3:2000SEP08 1790 1852 forward 2 TM N in 190 LI:020726.3:2000SEP08 1874 1936 forward 2 TM N in 190 LI:020726.3:2000SEP08 1958 2020 forward 2 TM N in 191 LI:027209.1:2000SEP08 25 111 forward 1 TM N out 191 LI:027209.1:2000SEP08 1129 1203 forward 1 TM N out 191 LI:027209.1:2000SEP08 1219 1305 forward 1 TM N out 191 LI:027209.1:2000SEP08 1447 1533 forward 1 TM N out 191 LI:027209.1:2000SEP08 413 475 forward 2 TM N out 191 LI:027209.1:2000SEP08 527 601 forward 2 TM N out 191 LI:027209.1:2000SEP08 659 739 forward 2 TM N out 191 LI:027209.1:2000SEP08 785 847 forward 2 TM N out 191 LI:027209.1:2000SEP08 1178 1234 forward 2 TM N out 191 LI:027209.1:2000SEP08 1232 1309 forward 2 TM N out 191 LI:027209.1:2000SEP08 1379 1465 forward 2 TM N out 191 LI:027209.1:2000SEP08 510 563 forward 3 TM N in 191 LI:027209.1:2000SEP08 882 938 forward 3 TM N in 191 LI:027209.1:2000SEP08 945 1016 forward 3 TM N in 191 LI:027209.1:2000SEP08 1041 1112 forward 3 TM N in 191 LI:027209.1:2000SEP08 1146 1208 forward 3 TM N in 191 LI:027209.1:2000SEP08 1224 1286 forward 3 TM N in 192 LI:108819.1:2000SEP08 196 264 forward 1 TM N in 192 LI:108819.1:2000SEP08 203 271 forward 2 TM 192 LI:108819.1:2000SEP08 290 343 forward 2 TM 193 LI:021759.1:2000SEP08 133 186 forward 1 TM N out 193 LI:021759.1:2000SEP08 59 115 forward 2 TM N out 193 LI:021759.1:2000SEP08 495 581 forward 3 TM N in 193 LI:021759.1:2000SEP08 981 1067 forward 3 TM N in 194 LI:1165967.1:2000SEP08 323 403 forward 2 TM N out 195 LI:1166315.1:2000SEP08 693 749 forward 3 TM N out 196 LI:204626.1:2000SEP08 19 99 forward 1 TM N out 197 LI:801140.1:2000SEP08 421 498 forward 1 TM N in 198 LI:286639.1:2000SEP08 127 213 forward 1 TM N out 198 LI:286639.1:2000SEP08 982 1068 forward 1 TM N out 198 LI:286639.1:2000SEP08 1879 1944 forward 1 TM N out 198 LI:286639.1:2000SEP08 62 148 forward 2 TM N out 198 LI:286639.1:2000SEP08 965 1027 forward 2 TM N out 198 LI:286639.1:2000SEP08 1061 1123 forward 2 TM N out 198 LI:286639.1:2000SEP08 1589 1663 forward 2 TM N out 198 LI:286639.1:2000SEP08 1787 1873 forward 2 TM N out 198 LI:286639.1:2000SEP08 267 320 forward 3 TM N out 198 LI:286639.1:2000SEP08 1794 1847 forward 3 TM N out 199 LI:288905.4:2000SEP08 868 927 forward 1 TM N out 199 LI:288905.4:2000SEP08 1552 1638 forward 1 TM N out 199 LI:288905.4:2000SEP08 1913 1975 forward 2 TM N out 199 LI:288905.4:2000SEP08 2000 2062 forward 2 TM N out 199 LI:288905.4:2000SEP08 99 158 forward 3 TM N in 200 LI:332161.1:2000SEP08 1507 1587 forward 1 TM N in 200 LI:332161.1:2000SEP08 1663 1743 forward 1 TM N in 200 LI:332161.1:2000SEP08 2314 2400 forward 1 TM N in 200 LI:332161.1:2000SEP08 2890 2940 forward 1 TM N in 200 LI:332161.1:2000SEP08 776 835 forward 2 TM 200 LI:332161.1:2000SEP08 1340 1393 forward 2 TM 200 LI:332161.1:2000SEP08 1493 1579 forward 2 TM 200 LI:332161.1:2000SEP08 1637 1717 forward 2 TM 200 LI:332161.1:2000SEP08 1880 1966 forward 2 TM 200 LI:332161.1:2000SEP08 2075 2161 forward 2 TM 200 LI:332161.1:2000SEP08 2744 2818 forward 2 TM 200 LI:332161.1:2000SEP08 258 311 forward 3 TM N in 200 LI:332161.1:2000SEP08 1524 1610 forward 3 TM N in 200 LI:332161.1:2000SEP08 2025 2111 forward 3 TM N in 200 LI:332161.1:2000SEP08 2289 2375 forward 3 TM N in 201 LI:184867.1:2000SEP08 1985 2041 forward 2 TM N in 201 LI:184867.1:2000SEP08 771 854 forward 3 TM N out 202 LI:229932.4:2000SEP08 76 162 forward 1 TM N out 202 LI:229932.4:2000SEP08 229 300 forward 1 TM N out 202 LI:229932.4:2000SEP08 1249 1329 forward 1 TM N out 202 LI:229932.4:2000SEP08 1438 1524 forward 1 TM N out 202 LI:229932.4:2000SEP08 1678 1764 forward 1 TM N out 202 LI:229932.4:2000SEP08 68 142 forward 2 TM N out 202 LI:229932.4:2000SEP08 215 271 forward 2 TM N out 202 LI:229932.4:2000SEP08 734 820 forward 2 TM N out 202 LI:229932.4:2000SEP08 1220 1291 forward 2 TM N out 202 LI:229932.4:2000SEP08 1565 1618 forward 2 TM N out 202 LI:229932.4:2000SEP08 60 146 forward 3 TM 202 LI:229932.4:2000SEP08 348 425 forward 3 TM 202 LI:229932.4:2000SEP08 762 848 forward 3 TM 202 LI:229932.4:2000SEP08 1239 1325 forward 3 TM 202 LI:229932.4:2000SEP08 1401 1487 forward 3 TM 202 LI:229932.4:2000SEP08 1629 1703 forward 3 TM 203 LI:1189932.1:2000SEP08 277 363 forward 1 TM N out 203 LI:1189932.1:2000SEP08 1141 1203 forward 1 TM N out 203 LI:1189932.1:2000SEP08 1216 1278 forward 1 TM N out 203 LI:1189932.1:2000SEP08 1411 1497 forward 1 TM N out 203 LI:1189932.1:2000SEP08 1642 1707 forward 1 TM N out 203 LI:1189932.1:2000SEP08 1795 1881 forward 1 TM N out 203 LI:1189932.1:2000SEP08 2125 2211 forward 1 TM N out 203 LI:1189932.1:2000SEP08 89 151 forward 2 TM N in 203 LI:1189932.1:2000SEP08 218 304 forward 2 TM N in 203 LI:1189932.1:2000SEP08 320 388 forward 2 TM N in 203 LI:1189932.1:2000SEP08 386 451 forward 2 TM N in 203 LI:1189932.1:2000SEP08 572 643 forward 2 TM N in 203 LI:1189932.1:2000SEP08 1142 1222 forward 2 TM N in 203 LI:1189932.1:2000SEP08 1412 1498 forward 2 TM N in 203 LI:1189932.1:2000SEP08 1928 1990 forward 2 TM N in 203 LI:1189932.1:2000SEP08 2021 2107 forward 2 TM N in 203 LI:1189932.1:2000SEP08 2141 2227 forward 2 TM N in 203 LI:1189932.1:2000SEP08 522 608 forward 3 TM N out 203 LI:1189932.1:2000SEP08 858 944 forward 3 TM N out 203 LI:1189932.1:2000SEP08 1161 1247 forward 3 TM N out 203 LI:1189932.1:2000SEP08 1992 2066 forward 3 TM N out 203 LI:1189932.1:2000SEP08 2139 2210 forward 3 TM N out 204 LI:1076689.1:2000SEP08 43 114 forward 1 TM N in 204 LI:1076689.1:2000SEP08 326 373 forward 2 TM N in 205 LI:415181.2:2000SEP08 1033 1113 forward 1 TM N in 205 LI:415181.2:2000SEP08 1363 1434 forward 1 TM N in 205 LI:415181.2:2000SEP08 914 1000 forward 2 TM 206 LI:296358.1:2000SEP08 760 819 forward 1 TM N out 206 LI:296358.1:2000SEP08 997 1068 forward 1 TM N out 206 LI:296358.1:2000SEP08 1147 1233 forward 1 TM N out 206 LI:296358.1:2000SEP08 197 247 forward 2 TM N out 206 LI:296358.1:2000SEP08 356 442 forward 2 TM N out 207 LI:205186.3:2000SEP08 644 697 forward 2 TM N in 207 LI:205186.3:2000SEP08 812 877 forward 2 TM N in 208 LI:220537.2:2000SEP08 595 681 forward 1 TM N in 208 LI:220537.2:2000SEP08 1429 1515 forward 1 TM N in 208 LI:220537.2:2000SEP08 245 331 forward 2 TM N out 208 LI:220537.2:2000SEP08 362 415 forward 2 TM N out 208 LI:220537.2:2000SEP08 1058 1129 forward 2 TM N out 208 LI:220537.2:2000SEP08 1136 1222 forward 2 TM N out 208 LI:220537.2:2000SEP08 1472 1555 forward 2 TM N out 208 LI:220537.2:2000SEP08 1820 1897 forward 2 TM N out 208 LI:220537.2:2000SEP08 216 299 forward 3 TM N out 208 LI:220537.2:2000SEP08 447 509 forward 3 TM N out 208 LI:220537.2:2000SEP08 522 584 forward 3 TM N out 208 LI:220537.2:2000SEP08 624 686 forward 3 TM N out 208 LI:220537.2:2000SEP08 702 764 forward 3 TM N out 208 LI:220537.2:2000SEP08 1467 1553 forward 3 TM N out 208 LI:220537.2:2000SEP08 1806 1892 forward 3 TM N out 209 LI:248364.2:2000SEP08 439 495 forward 1 TM N out 210 LI:2048338.1:2000SEP08 268 354 forward 1 TM N in 210 LI:2048338.1:2000SEP08 385 459 forward 1 TM N in 210 LI:2048338.1:2000SEP08 541 591 forward 1 TM N in 210 LI:2048338.1:2000SEP08 281 358 forward 2 TM N in 211 LI:1185203.8:2000SEP08 73 135 forward 1 TM N out 211 LI:1185203.8:2000SEP08 148 210 forward 1 TM N out 211 LI:1185203.8:2000SEP08 226 294 forward 1 TM N out 212 LI:021770.3:2000SEP08 593 673 forward 2 TM N out 212 LI:021770.3:2000SEP08 348 434 forward 3 TM N in 212 LI:021770.3:2000SEP08 462 539 forward 3 TM N in 212 LI:021770.3:2000SEP08 564 641 forward 3 TM N in 212 LI:021770.3:2000SEP08 861 944 forward 3 TM N in 213 LI:1185841.1:2000SEP08 1132 1182 forward 1 TM N out 213 LI:1185841.1:2000SEP08 2434 2520 forward 1 TM N out 213 LI:1185841.1:2000SEP08 965 1030 forward 2 TM N in 213 LI:1185841.1:2000SEP08 2381 2437 forward 2 TM N in 214 LI:1181710.1:2000SEP08 221 307 forward 2 TM N out 215 LI:2048959.1:2000SEP08 262 318 forward 1 TM N out 216 LI:798494.1:2000SEP08 595 657 forward 1 TM N out 216 LI:798494.1:2000SEP08 670 732 forward 1 TM N out 216 LI:798494.1:2000SEP08 215 268 forward 2 TM N out 216 LI:798494.1:2000SEP08 12 62 forward 3 TM N out 216 LI:798494.1:2000SEP08 60 113 forward 3 TM N out 217 LI:2049223.1:2000SEP08 436 507 forward 1 TM N in 217 LI:2049223.1:2000SEP08 416 484 forward 2 TM N out 218 LI:1177833.1:2000SEP08 712 798 forward 1 TM N in 219 LI:2049267.1:2000SEP08 215 289 forward 2 TM N out 219 LI:2049267.1:2000SEP08 240 323 forward 3 TM N out 220 LI:1165939.1:2000SEP08 554 640 forward 2 TM 221 LI:1170958.1:2000SEP08 326 376 forward 2 TM N out 222 LI:1089827.1:2000SEP08 1507 1584 forward 1 TM N in 223 LI:792112.1:2000SEP08 818 892 forward 2 TM N in 223 LI:792112.1:2000SEP08 9 86 forward 3 TM 223 LI:792112.1:2000SEP08 669 755 forward 3 TM 223 LI:792112.1:2000SEP08 783 860 forward 3 TM 224 LI:282219.2:2000SEP08 661 732 forward 1 TM N out 224 LI:282219.2:2000SEP08 491 577 forward 2 TM N in 224 LI:282219.2:2000SEP08 659 745 forward 2 TM N in 224 LI:282219.2:2000SEP08 408 458 forward 3 TM N in 225 LI:1088010.2:2000SEP08 289 375 forward 1 TM N in 225 LI:1088010.2:2000SEP08 716 793 forward 2 TM N in 225 LI:1088010.2:2000SEP08 1229 1315 forward 2 TM N in 225 LI:1088010.2:2000SEP08 903 980 forward 3 TM N out 225 LI:1088010.2:2000SEP08 1002 1088 forward 3 TM N out 225 LI:1088010.2:2000SEP08 1185 1247 forward 3 TM N out 225 LI:1088010.2:2000SEP08 1272 1334 forward 3 TM N out 226 LI:1165276.1:2000SEP08 301 363 forward 1 TM N in 226 LI:1165276.1:2000SEP08 882 968 forward 3 TM N out 227 LI:1169524.2:2000SEP08 623 709 forward 2 TM 227 LI:1169524.2:2000SEP08 713 778 forward 2 TM 227 LI:1169524.2:2000SEP08 842 928 forward 2 TM 228 LI:1180255.1:2000SEP08 731 784 forward 2 TM N in 228 LI:1180255.1:2000SEP08 872 931 forward 2 TM N in 228 LI:1180255.1:2000SEP08 1199 1285 forward 2 TM N in 229 LI:1091903.1:2000SEP08 454 540 forward 1 TM N out 230 LI:1169219.1:2000SEP08 496 582 forward 1 TM N in 230 LI:1169219.1:2000SEP08 509 595 forward 2 TM N out 230 LI:1169219.1:2000SEP08 495 581 forward 3 TM 231 LI:2050313.1:2000SEP08 2605 2664 forward 1 TM N in 231 LI:2050313.1:2000SEP08 3229 3315 forward 1 TM N in 231 LI:2050313.1:2000SEP08 3412 3498 forward 1 TM N in 231 LI:2050313.1:2000SEP08 1886 1954 forward 2 TM N in 231 LI:2050313.1:2000SEP08 2654 2731 forward 2 TM N in 231 LI:2050313.1:2000SEP08 2924 2986 forward 2 TM N in 231 LI:2050313.1:2000SEP08 3029 3091 forward 2 TM N in 231 LI:2050313.1:2000SEP08 3482 3568 forward 2 TM N in 231 LI:2050313.1:2000SEP08 855 920 forward 3 TM N out 231 LI:2050313.1:2000SEP08 2445 2531 forward 3 TM N out 231 LI:2050313.1:2000SEP08 2646 2708 forward 3 TM N out 231 LI:2050313.1:2000SEP08 2721 2783 forward 3 TM N out 231 LI:2050313.1:2000SEP08 3114 3170 forward 3 TM N out 231 LI:2050313.1:2000SEP08 3504 3590 forward 3 TM N out 232 LI:209351.3:2000SEP08 586 645 forward 1 TM N in 232 LI:209351.3:2000SEP08 1945 2025 forward 1 TM N in 232 LI:209351.3:2000SEP08 353 415 forward 2 TM 232 LI:209351.3:2000SEP08 665 718 forward 2 TM 232 LI:209351.3:2000SEP08 1313 1387 forward 2 TM 232 LI:209351.3:2000SEP08 1991 2041 forward 2 TM 232 LI:209351.3:2000SEP08 2153 2230 forward 2 TM 232 LI:209351.3:2000SEP08 2390 2443 forward 2 TM 232 LI:209351.3:2000SEP08 801 869 forward 3 TM N in 232 LI:209351.3:2000SEP08 1926 2006 forward 3 TM N in 232 LI:209351.3:2000SEP08 2382 2456 forward 3 TM N in 233 LI:119900.1:2000SEP08 667 744 forward 1 TM N in 233 LI:119900.1:2000SEP08 521 607 forward 2 TM N out 233 LI:119900.1:2000SEP08 719 799 forward 2 TM N out 233 LI:119900.1:2000SEP08 24 98 forward 3 TM 233 LI:119900.1:2000SEP08 678 764 forward 3 TM 234 LI:2052274.1:2000SEP08 332 418 forward 2 TM N in 234 LI:2052274.1:2000SEP08 1526 1612 forward 2 TM N in 234 LI:2052274.1:2000SEP08 939 1025 forward 3 TM N in 234 LI:2052274.1:2000SEP08 1500 1586 forward 3 TM N in 235 LI:1075502.1:2000SEP08 200 277 forward 2 TM N in 235 LI:1075502.1:2000SEP08 483 569 forward 3 TM N in 236 LI:813697.1:2000SEP08 805 867 forward 1 TM 236 LI:813697.1:2000SEP08 224 283 forward 2 TM 236 LI:813697.1:2000SEP08 1638 1715 forward 3 TM N out 236 LI:813697.1:2000SEP08 1722 1808 forward 3 TM N out 237 LI:814261.1:2000SEP08 562 618 forward 1 TM 237 LI:814261.1:2000SEP08 287 343 forward 2 TM N out 237 LI:814261.1:2000SEP08 512 598 forward 2 TM N out 237 LI:814261.1:2000SEP08 279 356 forward 3 TM N out 237 LI:814261.1:2000SEP08 474 557 forward 3 TM N out 238 LI:775334.1:2000SEP08 898 984 forward 1 TM N in 238 LI:775334.1:2000SEP08 581 661 forward 2 TM N out 239 LI:1180325.1:2000SEP08 833 919 forward 2 TM N in 240 LI:1183147.3:2000SEP08 268 342 forward 1 TM N in 240 LI:1183147.3:2000SEP08 370 456 forward 1 TM N in 240 LI:1183147.3:2000SEP08 712 798 forward 1 TM N in 240 LI:1183147.3:2000SEP08 937 1023 forward 1 TM N in 240 LI:1183147.3:2000SEP08 374 460 forward 2 TM N in 240 LI:1183147.3:2000SEP08 800 871 forward 2 TM N in 240 LI:1183147.3:2000SEP08 968 1045 forward 2 TM N in 240 LI:1183147.3:2000SEP08 1385 1450 forward 2 TM N in 240 LI:1183147.3:2000SEP08 156 224 forward 3 TM N out 240 LI:1183147.3:2000SEP08 285 347 forward 3 TM N out 240 LI:1183147.3:2000SEP08 414 500 forward 3 TM N out 240 LI:1183147.3:2000SEP08 687 770 forward 3 TM N out 240 LI:1183147.3:2000SEP08 846 932 forward 3 TM N out 240 LI:1183147.3:2000SEP08 1002 1067 forward 3 TM N out 241 LI:1175373.3:2000SEP08 283 357 forward 1 TM N out 242 LI:813757.1:2000SEP08 744 827 forward 3 TM N in 243 LI:1182979.2:2000SEP08 370 456 forward 1 TM N in 243 LI:1182979.2:2000SEP08 742 828 forward 1 TM N in 243 LI:1182979.2:2000SEP08 705 767 forward 3 TM N out 243 LI:1182979.2:2000SEP08 783 845 forward 3 TM N out 244 LI:1177823.2:2000SEP08 307 393 forward 1 TM N out 244 LI:1177823.2:2000SEP08 311 370 forward 2 TM N in 245 LI:1174279.1:2000SEP08 634 720 forward 1 TM N out 245 LI:1174279.1:2000SEP08 724 789 forward 1 TM N out 246 LI:1178411.1:2000SEP08 1357 1443 forward 1 TM 246 LI:1178411.1:2000SEP08 1290 1376 forward 3 TM N in 246 LI:1178411.1:2000SEP08 1419 1472 forward 3 TM N in 247 LI:1182739.1:2000SEP08 853 939 forward 1 TM N in 247 LI:1182739.1:2000SEP08 1900 1986 forward 1 TM N in 247 LI:1182739.1:2000SEP08 2131 2217 forward 1 TM N in 247 LI:1182739.1:2000SEP08 2341 2403 forward 1 TM N in 247 LI:1182739.1:2000SEP08 2446 2508 forward 1 TM N in 247 LI:1182739.1:2000SEP08 803 859 forward 2 TM N in 247 LI:1182739.1:2000SEP08 1268 1351 forward 2 TM N in 247 LI:1182739.1:2000SEP08 1445 1513 forward 2 TM N in 247 LI:1182739.1:2000SEP08 1796 1882 forward 2 TM N in 247 LI:1182739.1:2000SEP08 2090 2176 forward 2 TM N in 247 LI:1182739.1:2000SEP08 2267 2323 forward 2 TM N in 247 LI:1182739.1:2000SEP08 2363 2449 forward 2 TM N in 247 LI:1182739.1:2000SEP08 1182 1244 forward 3 TM N out 247 LI:1182739.1:2000SEP08 1254 1316 forward 3 TM N out 247 LI:1182739.1:2000SEP08 2100 2156 forward 3 TM N out 247 LI:1182739.1:2000SEP08 2301 2387 forward 3 TM N out 248 LI:234937.4:2000SEP08 301 387 forward 1 TM N out 249 LI:1170660.1:2000SEP08 604 690 forward 1 TM N in 249 LI:1170660.1:2000SEP08 757 843 forward 1 TM N in 249 LI:1170660.1:2000SEP08 937 990 forward 1 TM N in 249 LI:1170660.1:2000SEP08 1111 1179 forward 1 TM N in 249 LI:1170660.1:2000SEP08 512 583 forward 2 TM 249 LI:1170660.1:2000SEP08 911 973 forward 2 TM 249 LI:1170660.1:2000SEP08 986 1048 forward 2 TM 249 LI:1170660.1:2000SEP08 252 323 forward 3 TM N out 249 LI:1170660.1:2000SEP08 591 677 forward 3 TM N out 249 LI:1170660.1:2000SEP08 774 860 forward 3 TM N out 250 LI:1144409.1:2000SEP08 25 81 forward 1 TM N out 250 LI:1144409.1:2000SEP08 1708 1782 forward 1 TM N out 250 LI:1144409.1:2000SEP08 2281 2367 forward 1 TM N out 250 LI:1144409.1:2000SEP08 1658 1744 forward 2 TM N in 250 LI:1144409.1:2000SEP08 1880 1927 forward 2 TM N in 250 LI:1144409.1:2000SEP08 2294 2380 forward 2 TM N in 250 LI:1144409.1:2000SEP08 1614 1697 forward 3 TM N in 250 LI:1144409.1:2000SEP08 2217 2303 forward 3 TM N in 251 LI:246290.10:2000SEP08 248 304 forward 2 TM N out 251 LI:246290.10:2000SEP08 641 727 forward 2 TM N out 251 LI:246290.10:2000SEP08 3 89 forward 3 TM N out 252 LI:280034.1:2000SEP08 279 365 forward 3 TM N out

[0304] TABLE 5 SEQ ID NO: Template ID Component ID Start Stop 1 LG:150318.1:2000SEP08 482540R6 1 350 1 LG:150318.1:2000SEP08 482540H1 1 238 1 LG:150318.1:2000SEP08 6021134T8 126 531 1 LG:150318.1:2000SEP08 6021134R8 126 537 1 LG:150318.1:2000SEP08 6021134H1 126 629 2 LG:022529.1:2000SEP08 7593029H1 1 521 2 LG:022529.1:2000SEP08 g1645695 112 517 2 LG:022529.1:2000SEP08 2160267H1 275 514 2 LG:022529.1:2000SEP08 5284828H1 309 583 2 LG:022529.1:2000SEP08 g1880347 313 601 2 LG:022529.1:2000SEP08 7352207H1 330 707 2 LG:022529.1:2000SEP08 6863346H1 339 830 2 LG:022529.1:2000SEP08 3351341H1 423 681 2 LG:022529.1:2000SEP08 077299H1 432 632 2 LG:022529.1:2000SEP08 078146H1 438 646 2 LG:022529.1:2000SEP08 3801790F6 523 1030 2 LG:022529.1:2000SEP08 3801790H1 523 823 2 LG:022529.1:2000SEP08 3769238F6 523 1043 2 LG:022529.1:2000SEP08 3802590H1 524 810 2 LG:022529.1:2000SEP08 6217218H1 549 1039 2 LG:022529.1:2000SEP08 g5743872 664 1137 2 LG:022529.1:2000SEP08 g3051534 685 1047 2 LG:022529.1:2000SEP08 g4195758 789 1045 3 LG:352559.1:2000SEP08 6453567H1 1 503 3 LG:352559.1:2000SEP08 4052122H1 185 457 3 LG:352559.1:2000SEP08 4052122F7 185 636 3 LG:352559.1:2000SEP08 g3897399 255 371 4 LG:175223.1:2000SEP08 3081155F6 1 417 4 LG:175223.1:2000SEP08 3081155H1 2 315 4 LG:175223.1:2000SEP08 3081155T6 31 465 4 LG:175223.1:2000SEP08 g1648354 58 457 4 LG:175223.1:2000SEP08 5800009H1 99 507 5 LG:476989.1:2000SEP08 6874941H1 1 169 5 LG:476989.1:2000SEP08 6874955H1 1 204 5 LG:476989.1:2000SEP08 g4393499 51 432 5 LG:476989.1:2000SEP08 g4190810 96 432 6 LG:253268.7:2000SEP08 6772515H1 607 1083 6 LG:253268.7:2000SEP08 g5526194 596 941 6 LG:253268.7:2000SEP08 g4729197 690 941 6 LG:253268.7:2000SEP08 g5809986 501 941 6 LG:253268.7:2000SEP08 g2540947 535 937 6 LG:253268.7:2000SEP08 g922062 586 935 6 LG:253268.7:2000SEP08 6772515J1 454 961 6 LG:253268.7:2000SEP08 2535554F6 493 929 6 LG:253268.7:2000SEP08 g4392225 520 923 6 LG:253268.7:2000SEP08 g3424830 561 923 6 LG:253268.7:2000SEP08 g4533991 464 923 6 LG:253268.7:2000SEP08 g885146 693 914 6 LG:253268.7:2000SEP08 g917418 564 914 6 LG:253268.7:2000SEP08 g888754 605 914 6 LG:253268.7:2000SEP08 g922196 606 913 6 LG:253268.7:2000SEP08 g888391 595 912 6 LG:253268.7:2000SEP08 g5364213 457 897 6 LG:253268.7:2000SEP08 g990349 560 886 6 LG:253268.7:2000SEP08 g888707 589 884 6 LG:253268.7:2000SEP08 g885121 574 884 6 LG:253268.7:2000SEP08 g888978 669 883 6 LG:253268.7:2000SEP08 g990350 535 881 6 LG:253268.7:2000SEP08 6852955H1 306 854 6 LG:253268.7:2000SEP08 7236518H1 249 789 6 LG:253268.7:2000SEP08 2535554H1 493 737 6 LG:253268.7:2000SEP08 g889930 353 601 6 LG:253268.7:2000SEP08 g888417 353 587 6 LG:253268.7:2000SEP08 5773584H1 69 569 6 LG:253268.7:2000SEP08 488757R1 1 536 7 LG:401322.1:2000SEP08 4875149T6 344 737 7 LG:401322.1:2000SEP08 g3202357 457 784 7 LG:401322.1:2000SEP08 748032H1 574 776 7 LG:401322.1:2000SEP08 750543H1 1 183 7 LG:401322.1:2000SEP08 g1474315 42 323 7 LG:401322.1:2000SEP08 3722596H1 61 333 7 LG:401322.1:2000SEP08 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LI:1182739.1:2000SEP08 71225789V1 218 803 247 LI:1182739.1:2000SEP08 71225363V1 356 802 247 LI:1182739.1:2000SEP08 g1230045 567 750 247 LI:1182739.1:2000SEP08 71260619V1 154 715 247 LI:1182739.1:2000SEP08 71226125V1 98 693 247 LI:1182739.1:2000SEP08 71226227V1 116 689 247 LI:1182739.1:2000SEP08 8065473J1 1 669 247 LI:1182739.1:2000SEP08 70856031V1 154 661 247 LI:1182739.1:2000SEP08 70856138V1 154 474 247 LI:1182739.1:2000SEP08 6997551H1 2225 2640 247 LI:1182739.1:2000SEP08 g1231257 2295 2486 247 LI:1182739.1:2000SEP08 g564488 2212 2485 247 LI:1182739.1:2000SEP08 453607F1 1886 2485 247 LI:1182739.1:2000SEP08 g1928091 2175 2485 247 LI:1182739.1:2000SEP08 g4334289 2055 2484 248 LI:234937.4:2000SEP08 70200118V1 198 565 248 LI:234937.4:2000SEP08 6821993J1 1 276 248 LI:234937.4:2000SEP08 6821993H1 1 277 248 LI:234937.4:2000SEP08 1368116R7 27 230 248 LI:234937.4:2000SEP08 1368116H1 27 178 248 LI:234937.4:2000SEP08 6201371H1 28 589 248 LI:234937.4:2000SEP08 6444066H1 86 619 248 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70200111V1 182 708 248 LI:234937.4:2000SEP08 6439781H1 198 708 248 LI:234937.4:2000SEP08 70169923V1 386 666 248 LI:234937.4:2000SEP08 70200182V1 391 835 248 LI:234937.4:2000SEP08 4245558H1 421 665 248 LI:234937.4:2000SEP08 984607H1 440 753 248 LI:234937.4:2000SEP08 4194365H1 442 750 249 LI:1170660.1:2000SEP08 7582236H1 1 568 249 LI:1170660.1:2000SEP08 60218360D1 45 533 249 LI:1170660.1:2000SEP08 60218356D1 69 309 249 LI:1170660.1:2000SEP08 5547632H1 223 419 249 LI:1170660.1:2000SEP08 7186676H1 223 780 249 LI:1170660.1:2000SEP08 4706707H1 229 494 249 LI:1170660.1:2000SEP08 4543751H1 229 492 249 LI:1170660.1:2000SEP08 g1635530 251 552 249 LI:1170660.1:2000SEP08 g1230443 257 449 249 LI:1170660.1:2000SEP08 60218359D1 264 759 249 LI:1170660.1:2000SEP08 172943H1 324 547 249 LI:1170660.1:2000SEP08 60218364D1 513 923 249 LI:1170660.1:2000SEP08 4572811H1 588 716 249 LI:1170660.1:2000SEP08 7328676H1 604 1045 249 LI:1170660.1:2000SEP08 g706516 643 871 249 LI:1170660.1:2000SEP08 g883656 644 1014 249 LI:1170660.1:2000SEP08 3806727H1 649 774 249 LI:1170660.1:2000SEP08 g675102 664 1020 249 LI:1170660.1:2000SEP08 60218358D1 851 1293 249 LI:1170660.1:2000SEP08 4717311H1 889 1122 250 LI:1144409.1:2000SEP08 70858332V1 2057 2461 250 LI:1144409.1:2000SEP08 2101604H1 2028 2294 250 LI:1144409.1:2000SEP08 2101604R6 2028 2532 250 LI:1144409.1:2000SEP08 71225088V1 2034 2378 250 LI:1144409.1:2000SEP08 g2016400 2051 2147 250 LI:1144409.1:2000SEP08 71224917V1 2055 2615 250 LI:1144409.1:2000SEP08 804149H1 2058 2162 250 LI:1144409.1:2000SEP08 8095372H1 1450 1744 250 LI:1144409.1:2000SEP08 3814709H1 1477 1746 250 LI:1144409.1:2000SEP08 g2809907 2239 2430 250 LI:1144409.1:2000SEP08 496959H1 2271 2449 250 LI:1144409.1:2000SEP08 g1927355 2303 2606 250 LI:1144409.1:2000SEP08 70856122V1 2062 2396 250 LI:1144409.1:2000SEP08 g2540261 2063 2448 250 LI:1144409.1:2000SEP08 71227124V1 1448 1593 250 LI:1144409.1:2000SEP08 4556204H1 1561 1642 250 LI:1144409.1:2000SEP08 4551845F6 1561 1744 250 LI:1144409.1:2000SEP08 4265753H1 513 695 250 LI:1144409.1:2000SEP08 4337528F6 583 991 250 LI:1144409.1:2000SEP08 4337528H1 583 841 250 LI:1144409.1:2000SEP08 2792488H1 853 1139 250 LI:1144409.1:2000SEP08 2790452H2 853 1006 250 LI:1144409.1:2000SEP08 2792488F6 853 1240 250 LI:1144409.1:2000SEP08 71225608V1 853 1382 250 LI:1144409.1:2000SEP08 8045106H1 977 1635 250 LI:1144409.1:2000SEP08 7269729H1 1056 1608 250 LI:1144409.1:2000SEP08 7617315H1 1 258 250 LI:1144409.1:2000SEP08 4841542H1 12 274 250 LI:1144409.1:2000SEP08 7609838J1 42 593 250 LI:1144409.1:2000SEP08 7617315J1 307 888 250 LI:1144409.1:2000SEP08 76541 74H1 356 465 250 LI:1144409.1:2000SEP08 7697207H1 399 860 250 LI:1144409.1:2000SEP08 7697207J1 399 886 250 LI:1144409.1:2000SEP08 7608868J1 407 762 250 LI:1144409.1:2000SEP08 8045106J1 427 867 250 LI:1144409.1:2000SEP08 630611H1 2382 2607 250 LI:1144409.1:2000SEP08 904646R2 2397 2601 250 LI:1144409.1:2000SEP08 904646H1 2398 2608 250 LI:1144409.1:2000SEP08 2130512H1 2412 2606 250 LI:1144409.1:2000SEP08 4383061H1 2412 2583 250 LI:1144409.1:2000SEP08 g5632630 2501 2607 250 LI:1144409.1:2000SEP08 406063H1 2316 2543 250 LI:1144409.1:2000SEP08 7335618H1 2331 2616 250 LI:1144409.1:2000SEP08 g4329276 2347 2613 250 LI:1144409.1:2000SEP08 3219963H1 2062 2228 250 LI:1144409.1:2000SEP08 3485587H1 2062 2165 250 LI:1144409.1:2000SEP08 6020943H 1 2062 2430 250 LI:1144409.1:2000SEP08 70857496V1 1351 1744 250 LI:1144409.1:2000SEP08 8093771H1 1426 1744 250 LI:1144409.1:2000SEP08 505559H1 2150 2362 250 LI:1144409.1:2000SEP08 2792488T6 2157 2565 250 LI:1144409.1:2000SEP08 632101H1 2161 2424 250 LI:1144409.1:2000SEP08 3479107H1 2175 2356 250 LI:1144409.1:2000SEP08 822341R1 2189 2449 250 LI:1144409.1:2000SEP08 822341H1 2189 2412 250 LI:1144409.1:2000SEP08 70388384D1 2198 2607 250 LI:1144409.1:2000SEP08 g3086258 2215 2609 250 LI:1144409.1:2000SEP08 2101604T6 2217 2565 250 LI:1144409.1:2000SEP08 636591H1 2217 2470 250 LI:1144409.1:2000SEP08 g3961700 2503 2607 250 LI:1144409.1:2000SEP08 71226556V1 1132 1744 250 LI:1144409.1:2000SEP08 71225104V1 1161 1744 250 LI:1144409.1:2000SEP08 g1802842 1156 1515 250 LI:1144409.1:2000SEP08 71226355V1 1220 1744 250 LI:1144409.1:2000SEP08 5734055H1 1230 1497 250 LI:1144409.1:2000SEP08 71225770V1 1232 1744 250 LI:1144409.1:2000SEP08 70855263V1 1247 1744 250 LI:1144409.1:2000SEP08 70858102V1 1275 1762 250 LI:1144409.1:2000SEP08 6870517H1 1296 1814 250 LI:1144409.1:2000SEP08 71225590V1 1349 1744 250 LI:1144409.1:2000SEP08 g2011857 2103 2393 250 LI:1144409.1:2000SEP08 2875837H1 2116 2394 250 LI:1144409.1:2000SEP08 71226547V1 2122 2618 250 LI:1144409.1:20003EP08 g1849425 2131 2424 250 LI:1144409.1:2000SEP08 4337528T6 2144 2581 250 LI:1144409.1:2000SEP08 3118103F6 2146 2582 250 LI:1144409.1:2000SEP08 3118103H1 2147 2437 250 LI:1144409.1:2000SEP08 3814709F7 1498 1730 250 LI:1144409.1:2000SEP08 70854990V1 1522 1744 250 LI:1144409.1:2000SEP08 4557749H1 1561 1744 250 LI:1144409.1:2000SEP08 4556204F8 1561 2151 250 LI:1144409.1:2000SEP08 4557749F8 1580 2139 250 LI:1144409.1:2000SEP08 70856541V1 1580 1766 250 LI:1144409.1:2000SEP08 70856732V1 1601 1744 250 LI:1144409.1:2000SEP08 70858292V1 1605 2254 250 LI:1144409.1:2000SEP08 70856003V1 1634 2192 250 LI:1144409.1:2000SEP08 70857442V1 1649 1744 250 LI:1144409.1:2000SEP08 8038711H1 1794 2407 250 LI:1144409.1:2000SEP08 3999943H1 2062 2229 250 LI:1144409.1:2000SEP08 6147820H1 2078 2363 250 LI:1144409.1:2000SEP08 71225849V1 2080 2376 250 LI:1144409.1:2000SEP08 71225565V1 2080 2316 250 LI:1144409.1:2000SEP08 4445313H1 2080 2266 250 LI:1144409.1:2000SEP08 955100T2 2090 2570 250 LI:1144409.1:2000SEP08 955100R1 2090 2453 250 LI:1144409.1:2000SEP08 955100H1 2090 2358 250 LI:1144409.1:2000SEP08 3814175T6 2095 2570 251 LI:246290.10:2000SEP08 7160791H1 485 997 251 LI:246290.10:2000SEP08 1320454H1 499 734 251 LI:246290.10:2000SEP08 7644139J1 512 1059 251 LI:246290.10:2000SEP08 6723259H1 516 916 251 LI:246290.10:2000SEP08 747973R6 330 859 251 LI:246290.10:2000SEP08 747973H1 330 572 251 LI:246290.10:2000SEP08 7170570H1 383 910 251 LI:246290.10:2000SEP08 5080008H1 88 328 251 LI:246290.10:2000SEP08 5957953H1 89 545 251 LI:246290.10:2000SEP08 6937991H1 99 200 251 LI:246290.10:2000SEP08 7168155H1 137 243 251 LI:246290.10:2000SEP08 4831526F8 229 767 251 LI:246290.10:2000SEP08 4831526H1 230 359 251 LI:246290.10:2000SEP08 4831526F9 229 744 251 LI:246290.10:2000SEP08 7387420H1 285 504 251 LI:246290.10:2000SEP08 5761576H1 540 807 251 LI:246290.10:2000SEP08 4930979H1 612 891 251 LI:246290.10:2000SEP08 806868H1 728 958 251 LI:246290.10:2000SEP08 6866060H1 68 403 251 LI:246290.10:2000SEP08 3506257H1 73 350 251 LI:246290.10:2000SEP08 3550395H1 1 288 251 LI:246290.10:2000SEP08 7988114H1 2 511 251 LI:246290.10:2000SEP08 3316757H1 18 304 251 LI:246290.10:2000SEP08 8122994H1 19 612 251 LI:246290.10:2000SEP08 5457648H1 23 233 251 LI:246290.10:2000SEP08 3508411H1 23 303 251 LI:246290.10:2000SEP08 3577541H1 23 287 251 LI:246290.10:2000SEP08 5460535H1 23 271 251 LI:246290.10:2000SEP08 7002420H1 39 596 251 LI:246290.10:2000SEP08 4328953H1 42 304 251 LI:246290.10:2000SEP08 3973335H1 57 325 251 LI:246290.10:2000SEP08 7470753H1 67 633 251 LI:246290.10:2000SEP08 2966230H1 1 297 251 LI:246290.10:2000SEP08 2966230F6 1 377 252 LI:280034.1:2000SEP08 8045415H1 1 646 252 LI:280034.1:2000SEP08 8045415J1 482 1096 252 LI:280034.1:2000SEP08 681866T6 584 802 252 LI:280034.1:2000SEP08 681866H1 584 845 252 LI:280034.1:2000SEP08 681866R6 584 841 252 LI:280034.1:2000SEP08 4936924H1 781 1020

[0305] TABLE 6 SEQ ID NO: Template ID Tissue Distribution 1 LG:150318.1:2000SEP08 Nervous System - 100% 2 LG:022529.1:2000SEP08 Musculoskeletal System - 25%, Unclassified/Mixed - 22%, Cardiovascular System - 14% 3 LG:352559.1:2000SEP08 Unclassified/Mixed - 67%, Digestive System - 33% 4 LG:175223.1:2000SEP08 Embryonic Structures - 82%, Nervous System - 18% 5 LG:476989.1:2000SEP08 Exocrine Glands - 62%, Urinary Tract - 31% 6 LG:253268.7:2000SEP08 Germ Cells - 56%, Nervous System - 23% 7 LG:401322.1:2000SEP08 Sense Organs - 50%, Liver - 17%, Skin - 13% 8 LG:1328436.1:2000SEP08 Respiratory System - 38%, Endocrine System - 35%, Connective Tissue - 27% 9 LG:475404.1:2000SEP08 Skin - 81% 10 LG:1384132.1:2000SEP08 Respiratory System - 50%, Digestive System - 33%, Nervous System - 17% 11 LG:410804.18:2000SEP08 Nervous System - 100% 12 LG:1082306.1:2000SEP08 Cardiovascular System - 28%, Digestive System - 21%, Exocrine Glands - 14%, Endocrine System - 14% 13 LG:233814.4:2000SEP08 Endocrine System - 36%, Pancreas - 36%, Exocrine Glands - 16% 14 LG:977478.5:2000SEP08 Cardiovascular System - 34%, Musculoskeletal System - 19%, Female Genitalia - 16% 15 LG:025931.1:2000SEP08 Female Genitalia - 29%, Urinary Tract - 24%, Endocrine System - 24% 16 LG:885368.1:2000SEP08 Nervous System - 67%, Female Genitalia - 33% 17 LG:1054900.1:2000SEP08 Digestive System - 50%, Female Genitalia - 25%, Male Genitalia - 25% 18 LG:995186.2:2000SEP08 Digestive System - 67%, Nervous System - 33% 19 LG:435048.23:2000SEP08 Urinary Tract - 80%, Nervous System - 20% 20 LG:954859.1:2000SEP08 Embryonic Structures - 56%, Hemic and Immune System - 19%, Female Genitalia - 13%, Nervous System - 13% 21 LG:364370.1:2000SEP08 Liver - 90%, Male Genitalia - 10% 22 LG:1098789.1:2000SEP08 Urinary Tract - 100% 23 LG:201540.2:2000SEP08 Unclassified/Mixed - 15%, Female Genitalia - 13%, Connective Tissue - 13%, Male Genitalia - 13% 24 LG:1077357.1:2000SEP08 Nervous System - 43%, Male Genitalia - 29%, Female Genitalia - 29% 25 LG:1048846.4:2000SEP08 Female Genitalia - 25%, Digestive System - 25%, Male Genitalia - 25% 26 LG:336685.1:2000SEP08 Hemic and Immune System - 35%, Urinary Tract - 24%, Male Genitalia - 24% 27 LG:1076253.1:2000SEP08 Liver - 50%, Urinary Tract - 11%, Endocrine System - 11% 28 LG:1400601.2:2000SEP08 Skin - 100% 29 LG:1079092.3:2000SEP08 Musculoskeletal System - 100% 30 LG:1086064.1:2000SEP08 Skin - 69% 31 LG:1400608.1:2000SEP08 Female Genitalia - 26%, Urinary Tract - 21%, Respiratory System - 16% 32 LG:399275.5:2000SEP08 Respiratory System - 50%, Male Genitalia - 33%, Hemic and Immune System - 17% 33 LG:293943.1:2000SEP08 Exocrine Glands - 50%, Digestive System - 25%, Hemic and Immune System - 13%, Nervous System - 13% 34 LG:345884.1:2000SEP08 Respiratory System - 63%, Hemic and Immune System - 38% 35 LG:400967.1:2000SEP08 Embryonic Structures - 36%, Urinary Tract - 28%, Cardiovascular System - 16% 36 LG:024556.6:2000SEP08 Nervous System - 89%, Male Genitalia - 11% 37 LG:081189.3:2000SEP08 Germ Cells - 88% 38 LG:018258.1:2000SEP08 Digestive System - 44%, Endocrine System - 44%, Hemic and Immune System - 11% 39 LG:450399.3:2000SEP08 Nervous System - 100% 40 LG:451122.1:2000SEP08 Nervous System - 100% 41 LG:451682.1:2000SEP08 Nervous System - 100% 42 LG:238631.4:2000SEP08 Liver - 17%, Endocrine System - 14%, Respiratory System - 11%, Male Genitalia - 11% 43 LG:236654.1:2000SEP08 Unclassified/Mixed - 38%, Respiratory System - 15% 44 LG:332655.1:2000SEP08 Pancreas - 26%, Digestive System - 17%, Female Genitalia - 13% 45 LG:217396.2:2000SEP08 Skin - 24%, Embryonic Structures - 15%, Pancreas - 15% 46 LG:090574.1:2000SEP08 Respiratory System - 100% 47 LG:202943.1:2000SEP08 Embryonic Structures - 44%, Female Genitalia - 19%, Liver - 14% 48 LG:236928.1:2000SEP08 Unclassified/Mixed - 15%, Hemic and Immune System - 14%, Nervous System - 12% 49 LG:215169.2:2000SEP08 Endocrine System - 22%, Unclassified/Mixed - 20%, Nervous System - 20% 50 LG:410726.1:2000SEP08 Embryonic Structures - 38%, Pancreas - 24%, Endocrine System - 18% 51 LG:234372.2:2000SEP08 Stomatognathic System - 17%, Germ Cells - 12%, Musculoskeletal System - 11% 52 LG:022629.1:2000SEP08 Unclassified/Mixed - 36%, Germ Cells - 28% 53 LG:068682.1:2000SEP08 Unclassified/Mixed - 61%, Male Genitalia - 20% 54 LG:222335.1:2000SEP08 Musculoskeletal System - 27%, Exocrine Glands - 17%, Male Genitalia - 13% 55 LG:331342.1:2000SEP08 Male Genitalia - 35%, Digestive System - 22%, Endocrine System - 20% 56 LG:021770.1:2000SEP08 Pancreas - 18%, Exocrine Glands - 14%, Nervous System - 12%, Urinary Tract - 12%, Male Genitalia - 12% 57 LG:181607.9:2000SEP08 Musculoskeletal System - 25%, Cardiovascular System - 22%, Embryonic Structures - 18% 58 LG:1042768.1:2000SEP08 Liver - 100% 59 LG:282729.1:2000SEP08 Skin - 74%, Unclassified/Mixed - 21% 60 LG:998305.3:2000SEP08 Urinary Tract - 50%, Cardiovascular System - 29%, Nervous System - 21% 61 LG:1135213.1:2000SEP08 Embryonic Structures - 26%, Cardiovascular System - 20%, Digestive System - 11%, Unclassified/Mixed - 11% 62 LG:267762.1:2000SEP08 Cardiovascular System - 16%, Urinary Tract - 14%, Connective Tissue - 14% 63 LG:120744.1:2000SEP08 Skin - 35%, Embryonic Structures - 23%, Digestive System - 20% 64 LG:403409.1:2000SEP08 Stomatognathic System - 45%, Respiratory System - 12% 65 LG:226874.3:2000SEP08 Respiratory System - 38%, Male Genitalia - 35%, Female Genitalia - 19% 66 LG:1045521.4:2000SEP08 Germ Cells - 16% 67 LG:275876.1:2000SEP08 Unclassified/Mixed - 53%, Endocrine System - 27%, Nervous System - 20% 68 LG:475127.7:2000SEP08 Hemic and Immune System - 75%, Nervous System - 25% 69 LG:157263.1:2000SEP08 Embryonic Structures - 39%, Urinary Tract - 30% 70 LG:247382.7:2000SEP08 Urinary Tract - 19%, Hemic and Immune System - 13%, Embryonic Structures - 13%, Endocrine System - 13% 71 LG:197367.5:2000SEP08 Endocrine System - 100% 72 LG:218090.5:2000SEP08 Unclassified/Mixed - 42%, Urinary Tract - 21%, Exocrine Glands - 21% 73 LG:216612.4:2000SEP08 Nervous System - 45%, Digestive System - 30%, Endocrine System - 20% 74 LG:197614.1:2000SEP08 Germ Cells - 17%, Unclassified/Mixed - 16% 75 LG:378428.1:2000SEP08 Liver - 30%, Endocrine System - 15%, Embryonic Structures - 15% 76 LG:286639.1:2000SEP08 Germ Cells - 72% 77 LG:389870.1:2000SEP08 Liver - 41%, Nervous System - 23%, Cardiovascular System - 18%, Endocrine System - 18% 78 LG:1387485.6:2000SEP08 Female Genitalia - 16%, Digestive System - 14%, Urinary Tract - 13% 79 LG:230151.1:2000SEP08 Exocrine Glands - 16%, Urinary Tract - 14%, Liver - 12%, Pancreas - 12% 80 LG:215158.5:2000SEP08 Liver - 13%, Nervous System - 12%, Unclassified/Mixed - 11% 81 LG:235840.1:2000SEP08 Connective Tissue - 13%, Nervous System - 12%, Hemic and Immune System - 11%, Liver - 11% 82 LG:350272.1:2000SEP08 Germ Cells - 17%, Musculoskeletal System - 15% 83 LG:232190.1:2000SEP08 Liver - 24%, Unclassified/Mixed - 23%, Skin - 19% 84 LG:1068127.1:2000SEP08 Hemic and Immune System - 43%, Male Genitalia - 29%, Nervous System - 29% 85 LG:408751.3:2000SEP08 Nervous System - 43%, Sense Organs - 31% 86 LG:1078933.1:2000SEP08 Liver - 23%, Unclassified/Mixed - 20%, Nervous System - 13% 87 LG:958731.1:2000SEP08 Nervous System - 100% 88 LG:024125.5:2000SEP08 Connective Tissue - 17%, Embryonic Structures - 16% 89 LG:373637.3:2000SEP08 Unclassified/Mixed - 73%, Male Genitalia - 23% 90 LG:1053229.1:2000SEP08 Cardiovascular System - 50%, Embryonic Structures - 41% 91 LG:248364.1:2000SEP08 Sense Organs - 48%, Female Genitalia - 17% 92 LG:477130.1:2000SEP08 Nervous System - 100% 93 LG:113786.17:2000SEP08 Hemic and Immune System - 100% 94 LG:347635.1:2000SEP08 Musculoskeletal System - 45%, Female Genitalia - 17%, Urinary Tract - 14% 95 LG:242966.4:2000SEP08 Germ Cells - 23%, Stomatognathic System - 23% 96 LG:217814.1:2000SEP08 Skin - 25%, Liver - 16%, Unclassified/Mixed - 15% 97 LG:476452.1:2000SEP08 Nervous System - 100% 98 LG:1100657.1:2000SEP08 Liver - 100% 99 LG:1132418.2:2000SEP08 Cardiovascular System - 100% 100 LG:1098570.1:2000SEP08 Liver - 100% 101 LG:1097987.1:2000SEP08 Embryonic Structures - 41%, Musculoskeletal System - 27%, Female Genitalia - 23% 102 LG:337818.2:2000SEP08 Digestive System - 35%, Liver - 13%, Female Genitalia - 10% 103 LG:1040582.1:2000SEP08 Liver - 38%, Pancreas - 38%, Cardiovascular System - 17% 104 LG:1099122.1:2000SEP08 Liver - 96% 105 LG:1327449.1:2000SEP08 Endocrine System - 40%, Respiratory System - 30%, Digestive System - 20% 106 LG:227933.5:2000SEP08 Male Genitalia - 33%, Nervous System - 21%, Female Genitalia - 15% 107 LG:1043709.2:2000SEP08 Liver - 100% 108 LG:1099871.1:2000SEP08 Liver - 90%, Nervous System - 10% 109 LG:1399139.4:2000SEP08 Unclassified/Mixed - 30%, Male Genitalia - 26%, Musculoskeletal System - 22% 110 LG:236386.1:2000SEP08 Skin - 16%, Connective Tissue - 13%, Pancreas - 10% 111 LG:1015157.1:2000SEP08 Liver - 100% 112 LG:1065433.1:2000SEP08 Female Genitalia - 50%, Endocrine System - 40%, Nervous System - 10% 113 LG:236992.4:2000SEP08 Connective Tissue - 64%, Urinary Tract - 12%, Cardiovascular System - 12% 114 LG:1071124.1:2000SEP08 Unclassified/Mixed - 22%, Cardiovascular System - 22%, Urinary Tract - 19% 115 LG:206425.2:2000SEP08 Sense Organs - 39%, Female Genitalia - 10% 116 LG:885747.2:2000SEP08 Female Genitalia - 100% 117 LG:1140501.1:2000SEP08 Sense Organs - 20%, Nervous System - 15% 118 LG:001239.1:2000SEP08 Hemic and Immune System - 35%, Liver - 17%, Male Genitalia - 13% 119 LG:018980.1:2000SEP08 Unclassified/Mixed - 52%, Urinary Tract - 12%, Nervous System - 12% 120 LG:1083120.3:2000SEP08 Digestive System - 50%, Hemic and Immune System - 25%, Nervous System - 25% 121 LG:233258.3:2000SEP08 Germ Cells - 25%, Female Genitalia - 12% 122 LG:999062.1:2000SEP08 Nervous System - 100% 123 LG:887776.1:2000SEP08 Cardiovascular System - 35%, Skin - 33%, Hemic and Immune System - 14% 124 LG:1400301.2:2000SEP08 Exocrine Glands - 50%, Connective Tissue - 44% 125 LG:1329362.1:2000SEP08 Unclassified/Mixed - 44%, Urinary Tract - 22%, Exocrine Glands - 22% 126 LG:1096498.1:2000SEP08 Liver - 100% 127 LG:1096337.1:2000SEP08 Urinary Tract - 40%, Exocrine Glands - 40%, Nervous System - 20% 128 LG:1400579.1:2000SEP08 Liver - 53%, Musculoskeletal System - 25% 129 LG:1080091.1:2000SEP08 Connective Tissue - 21%, Musculoskeletal System - 18%, Female Genitalia - 15% 130 LG:1082203.1:2000SEP08 Embryonic Structures - 23%, Endocrine System - 11%, Male Genitalia - 11% 131 LG:1084051.1:2000SEP08 Germ Cells - 33%, Pancreas - 11%, Male Genitalia - 11% 132 LG:1082393.1:2000SEP08 Male Genitalia - 20%, Urinary Tract - 13%, Unclassified/Mixed - 13% 133 LG:1086183.1:2000SEP08 Liver - 25%, Skin - 20%, Hemic and Immune System - 14% 134 LG:1090268.1:2000SEP08 Sense Organs - 40%, Unclassified/Mixed - 17% 135 LG:1400597.5:2000SEP08 Unclassified/Mixed - 53%, Connective Tissue - 47% 136 LG:1080307.2:2000SEP08 Digestive System - 100% 137 LG:1400603.2:2000SEP08 Germ Cells - 40%, Nervous System - 18%, Unclassified/Mixed - 12% 138 LG:1052984.1:2000SEP08 Skin - 31%, Musculoskeletal System - 15%, Endocrine System - 10%, Pancreas - 10% 139 LG:1091259.1:2000SEP08 Connective Tissue - 66%, Respiratory System - 25% 140 LG:1082263.2:2000SEP08 Embryonic Structures - 32%, Endocrine System - 15%, Nervous System - 10% 141 LG:1048604.2:2000SEP08 Exocrine Glands - 50%, Embryonic Structures - 38% 142 LG:1085254.3:2000SEP08 Embryonic Structures - 61%, Respiratory System - 32% 143 LG:1400606.2:2000SEP08 Embryonic Structures - 34%, Unclassified/Mixed - 14%, Nervous System - 13%, Connective Tissue - 13% 144 LG:1090358.2:2000SEP08 Urinary Tract - 36%, Male Genitalia - 23%, Hemic and Immune System - 15%, Musculoskeletal System - 15% 145 LG:1079064.2:2000SEP08 Nervous System - 21%, Female Genitalia - 16%, Liver - 12% 146 LG:1076866.1:2000SEP08 Germ Cells - 28%, Embryonic Structures - 20%, Cardiovascular System - 12% 147 LG:969359.1:2000SEP08 Liver - 79%, Pancreas - 19% 148 LG:366783.1:2000SEP08 Sense Organs - 95% 149 LG:332176.3:2000SEP08 Pancreas - 28%, Connective Tissue - 22%, Urinary Tract - 22% 150 LG:994938.1:2000SEP08 Exocrine Glands - 50%, Respiratory System - 21%, Urinary Tract - 17% 151 LG:982800.1:2000SEP08 Urinary Tract - 22%, Skin - 21%, Germ Cells - 13% 152 LG:977850.7:2000SEP08 Exocrine Glands - 100% 153 LG:234748.2:2000SEP08 Sense Organs - 27%, Urinary Tract - 15%, Unclassified/Mixed - 11% 154 LG:306284.1:2000SEP08 Nervous System - 60%, Male Genitalia - 40% 155 LI:333170.3:2000SEP08 Germ Cells - 82%, Unclassified/Mixed - 13% 156 LI:336685.2:2000SEP08 Hemic and Immune System - 35%, Male Genitalia - 25%, Urinary Tract - 20% 157 LI:279013.5:2000SEP08 Female Genitalia - 100% 158 LI:1037075.1:2000SEP08 Musculoskeletal System - 94% 159 LI:1073403.1:2000SEP08 Liver - 100% 160 LI:1075296.1:2000SEP08 Liver - 100% 161 LI:1085501.1:2000SEP08 Connective Tissue - 100% 162 LI:1086181.1:2000SEP08 Liver - 100% 163 LI:1164493.1:2000SEP08 Urinary Tract - 52%, Female Genitalia - 20%, Digestive System - 12%, Male Genitalia - 12% 164 LI:1175097.1:2000SEP08 Unclassified/Mixed - 57%, Digestive System - 21%, Nervous System - 21% 165 LI:1092948.1:2000SEP08 Embryonic Structures - 26%, Connective Tissue - 19%, Musculoskeletal System - 17% 166 LI:380378.2:2000SEP08 Nervous System - 100% 167 LI:1029674.1:2000SEP08 Digestive System - 42%, Nervous System - 36%, Unclassified/Mixed - 22% 169 LI:1186208.1:2000SEP08 Stomatognathic System - 51%, Sense Organs - 38% 170 LI:1170753.1:2000SEP08 Endocrine System - 95% 171 LI:1180908.1:2000SEP08 Skin - 21%, Embryonic Structures - 14%, Male Genitalia - 13% 172 LI:1182900.2:2000SEP08 Digestive System - 47%, Pancreas - 34%, Respiratory System - 19% 173 LI:1169548.2:2000SEP08 Nervous System - 100% 174 LI:1039974.1:2000SEP08 Female Genitalia - 31%, Urinary Tract - 29%, Nervous System - 16% 175 LI:1175765.2:2000SEP08 Nervous System - 100% 176 LI:313948.1:2000SEP08 Unclassified/Mixed - 31%, Endocrine System - 23%, Cardiovascular System - 19% 177 LI:335923.2:2000SEP08 Germ Cells - 74%, Male Genitalia - 26% 178 LI:345884.1:2000SEP08 Respiratory System - 75%, Hemic and Immune System - 25% 179 LI:417127.1:2000SEP08 Connective Tissue - 100% 180 LI:451710.1:2000SEP08 Connective Tissue - 90%, Nervous System - 10% 181 LI:406882.2:2000SEP08 Sense Organs - 34%, Unclassified/Mixed - 15%, Nervous System - 15% 182 LI:728223.1:2000SEP08 Nervous System - 100% 183 LI:289783.19:2000SEP08 Digestive System - 38%, Unclassified/Mixed - 15%, Respiratory System - 12% 184 LI:235255.8:2000SEP08 Exocrine Glands - 23%, Connective Tissue - 12%, Female Genitalia - 11% 185 LI:237693.5:2000SEP08 Urinary Tract - 32%, Hemic and Immune System - 25%, Endocrine System - 21% 186 LI:433670.3:2000SEP08 Nervous System - 50%, Male Genitalia - 25%, Digestive System - 25% 187 LI:202943.4:2000SEP08 Embryonic Structures - 42%, Liver - 19%, Unclassified/Mixed - 16% 188 LI:068682.1:2000SEP08 Unclassified/Mixed - 47%, Digestive System - 21%, Male Genitalia - 19% 189 LI:203301.3:2000SEP08 Germ Cells - 19%, Male Genitalia - 14%, Respiratory System - 12% 190 LI:020726.3:2000SEP08 Sense Organs - 79% 191 LI:027209.1:2000SEP08 Musculoskeletal System - 53%, Female Genitalia - 27%, Exocrine Glands - 17% 192 LI:108819.1:2000SEP08 Urinary Tract - 45%, Digestive System - 28%, Skin - 15% 193 LI:021759.1:2000SEP08 Hemic and Immune System - 40%, Nervous System - 22%, Liver - 11% 194 LI:1165967.1:2000SEP08 Liver - 50%, Stomatognathic System - 50% 195 LI:1166315.1:2000SEP08 Cardiovascular System - 33%, Urinary Tract - 27%, Female Genitalia - 20%, Hemic and Immune System - 20% 196 LI:204626.1:2000SEP08 Digestive System - 58%, Nervous System - 15%, Exocrine Glands - 13% 197 LI:801140.1:2000SEP08 Embryonic Structures - 50%, Cardiovascular System - 38% 198 LI:286639.1:2000SEP08 Germ Cells - 64% 199 LI:288905.4:2000SEP08 Unclassified/Mixed - 76%, Nervous System - 24% 200 LI:332161.1:2000SEP08 Cardiovascular System - 47%, Nervous System - 14%, Connective Tissue - 10% 201 LI:184867.1:2000SEP08 Unclassified/Mixed - 33%, Embryonic Structures - 24%, Male Genitalia - 16% 202 LI:229932.4:2000SEP08 Musculoskeletal System - 40%, Cardiovascular System - 21% 203 LI:1189932.1:2000SEP08 Embryonic Structures - 37%, Germ Cells - 18%, Sense Organs - 13% 204 LI:1076689.1:2000SEP08 Liver - 99% 205 LI:415181.2:2000SEP08 Nervous System - 100% 206 LI:296358.1:2000SEP08 Hemic and Immune System - 83% 207 LI:205186.3:2000SEP08 Cardiovascular System - 59%, Male Genitalia - 20%, Unclassified/Mixed - 16% 208 LI:220537.2:2000SEP08 Stomatognathic System - 52%, Male Genitalia - 32% 209 LI:248364.2:2000SEP08 Cardiovascular System - 30%, Female Genitalia - 23%, Sense Organs - 22% 210 LI:2048338.1:2000SEP08 Connective Tissue - 90%, Nervous System - 10% 211 LI:1185203.8:2000SEP08 Nervous System - 75%, Female Genitalia - 25% 212 LI:021770.3:2000SEP08 Pancreas - 77% 213 LI:1185841.1:2000SEP08 Hemic and Immune System - 30%, Respiratory System - 26% 214 LI:1181710.1:2000SEP08 Male Genitalia - 38%, Nervous System - 38%, Hemic and Immune System - 25% 215 LI:2048959.1:2000SEP08 Musculoskeletal System - 73%, Endocrine System - 27% 216 LI:798494.1:2000SEP08 Germ Cells - 88% 217 LI:2049223.1:2000SEP08 Male Genitalia - 60%, Hemic and Immune System - 40% 218 LI:1177833.1:2000SEP08 Liver - 55%, Embryonic Structures - 10% 219 LI:2049267.1:2000SEP08 Cardiovascular System - 36%, Urinary Tract - 29%, Digestive System - 21% 220 LI:1165939.1:2000SEP08 Sense Organs - 62%, Endocrine System - 20% 221 LI:1170958.1:2000SEP08 Exocrine Glands - 53%, Cardiovascular System - 26%, Male Genitalia - 16% 222 LI:1089827.1:2000SEP08 Endocrine System - 16%, Male Genitalia - 13%, Musculoskeletal System - 12% 223 LI:792112.1:2000SEP08 Liver - 83% 224 LI:282219.2:2000SEP08 Embryonic Structures - 55%, Exocrine Glands - 23%, Male Genitalia - 14% 225 LI:1088010.2:2000SEP08 Exocrine Glands - 31%, Musculoskeletal System - 23%, Respiratory System - 13% 226 LI:1165276.1:2000SEP08 Nervous System - 18%, Male Genitalia - 16%, Pancreas - 16% 227 LI:1169524.2:2000SEP08 Endocrine System - 41%, Urinary Tract - 16%, Musculoskeletal System - 14%, Male Genitalia - 14% 228 LI:1180255.1:2000SEP08 Female Genitalia - 66%, Liver - 11%, Embryonic Structures - 11% 229 LI:1091903.1:2000SEP08 Germ Cells - 93% 230 LI:1169219.1:2000SEP08 Sense Organs - 34%, Skin - 22% 231 LI:2050313,1:2000SEP08 Skin - 15%, Respiratory System - 14%, Male Genitalia - 14% 232 LI:209351.3:2000SEP08 Cardiovascular System - 41% 233 LI:119900.1:2000SEP08 Stomatognathic System - 77% 234 LI:2052274.1:2000SEP08 Urinary Tract - 31%, Female Genitalia - 19%, Liver - 12% 235 LI:1075502.1:2000SEP08 Liver - 100% 236 LI:813697.1:2000SEP08 Endocrine System - 36%, Unclassified/Mixed - 25%, Exocrine Glands - 15% 237 LI:814261.1:2000SEP08 Exocrine Glands - 50%, Respiratory System - 20%, Urinary Tract - 13% 238 LI:775334.1:2000SEP08 Cardiovascular System - 26%, Embryonic Structures - 23%, Unclassified/Mixed - 15% 239 LI:1180325.1:2000SEP08 Skin - 38%, Pancreas - 23%, Female Genitalia - 23% 240 LI:1183147.3:2000SEP08 Female Genitalia - 42%, Respiratory System - 17%, Nervous System - 13% 241 LI:1175373.3:2000SEP08 Nervous System - 50%, Male Genitalia - 25%, Digestive System - 25% 242 LI:813757.1:2000SEP08 Female Genitalia - 50%, Nervous System - 50% 243 LI:1182979.2:2000SEP08 Respiratory System - 67%, Pancreas - 19% 244 LI:1177823.2:2000SEP08 Embryonic Structures - 48%, Cardiovascular System - 20%, Exocrine Glands - 20% 245 LI:1174279.1:2000SEP08 Endocrine System - 36%, Nervous System - 19%, Liver - 18% 246 LI:1178411.1:2000SEP08 Nervous System - 21%, Liver- 18%, Exocrine Glands - 15% 247 LI:1182739.1:2000SEP08 Unclassified/Mixed - 34%, Skin - 18%, Nervous System - 12% 248 LI:234937.4:2000SEP08 Endocrine System - 33%, Nervous System - 24%, Digestive System - 21% 249 LI:1170660.1:2000SEP08 Musculoskeletal System - 21%, Nervous System - 18%, Cardiovascular System - 13%, Male Genitalia - 13% 250 LI:1144409.1:2000SEP08 Sense Organs - 53% 251 LI:246290.10:2000SEP08 Cardiovascular System - 29%, Female Genitalia - 29% 252 LI:280034.1:2000SEP08 Female Genitalia - 100%

[0306] SEQ ID NO: Frame Length Start Stop GI Number Probability Score Annotation 253 2 114 2 343 g11643582 2.00E−68 PR-domain containing protein 14 253 2 114 2 343 g10434076 2.00E−68 unnamed protein product 253 2 114 2 343 g7020503 4.00E−27 unnamed protein product 255 2 211 2 634 g7243243 2.00E−43 KIAA1431 protein 255 2 211 2 634 g4567178 2.00E−41 R31665_2 (AA 1-673) 255 2 211 2 634 g3445181 2.00E−41 R31665_2 256 3 151 54 506 g10433955 5.00E−40 unnamed protein product 256 3 151 54 506 g7295442 4.00E−14 CG17334 gene product 256 3 151 54 506 g2073111 3.00E−11 Y box protein 2 257 2 138 17 430 g12407395 4.00E−54 tripartite motif protein TRIM7 257 2 138 17 430 g12407397 2.00E−42 tripartite motif protein TRIM7 257 2 138 17 430 g12407379 8.00E−16 tripartite motif protein TRIM4 isoform beta 258 1 317 1 951 g9246977 1.00E−137 RNA-binding protein BRUNOL4 258 1 317 1 951 g12746394 1.00E−136 CUG-BP and ETR-3 like factor 4 258 1 317 1 951 g13278792 1.00E−106 Bruno (Drosophila)-like 4, RNA binding protein 260 2 114 14 355 g4589588 2.00E−34 KIAA0972 protein 260 2 114 14 355 g7576272 2.00E−30 bA393J16.1 (zinc finger protein 33a (KOX 31)) 260 2 114 14 355 g498152 2.00E−30 ha0946 protein is Kruppel-related. 261 2 127 140 520 g10434195 2.00E−64 unnamed protein product 261 2 127 140 520 g13529188 4.00E−42 Unknown (protein for MGC: 12466) 261 2 127 140 520 g6467206 3.00E−36 gonadotropin inducible transcription repressor-4 262 1 151 1 453 g14042293 4.00E−47 unnamed protein product 262 1 151 1 453 g12052983 1.00E−46 hypothetical protein 262 1 151 1 453 g487785 7.00E−46 zinc finger protein ZNF136 263 1 79 16 252 g349075 4.00E−16 calmodulin-binding protein 263 1 79 16 252 g13543326 4.00E−16 hypothetical protein MGC8407 263 1 79 16 252 g12804937 4.00E−16 Unknown (protein for MGC: 3732) 264 1 183 112 660 g13325337 3.00E−83 Unknown (protein for MGC: 10520) 264 1 183 112 660 g8439407 3.00E−22 zinc finger protein 264 1 183 112 660 g7020166 3.00E−22 unnamed protein product 266 3 260 3 782 g12698001 1.00E−147 KIAA1728 protein 266 3 260 3 782 g8052233 1.00E−94 putative ankyrin-repeat containing protein 266 3 260 3 782 g7294632 2.00E−61 CG5679 gene product 267 2 196 2 589 g6249687 1.00E−108 P31155_1 267 2 196 2 589 g10436360 1.00E−53 unnamed protein product 267 2 196 2 589 g14042803 6.00E−50 unnamed protein product 268 1 113 130 468 g14596085 7.00E−55 (AY042830) Putative 40S ribosomal protein S15A 268 1 113 130 468 g9757906 7.00E−55 40S ribosomal protein S15A 268 1 113 130 468 g8439890 7.00E−55 Strong similarity to 40S ribosomal protein S15A from Arabidopsis thallana gb|L27461. EST gb|R30315 comes from this gene. 269 3 165 3 497 g12052983 2.00E−73 hypothetical protein 269 3 165 3 497 g5262560 1.00E−47 hypothetical protein 269 3 165 3 497 g10434856 1.00E−47 unnamed protein product 270 3 168 165 668 g12052983 4.00E−70 hypothetical protein 270 3 168 165 668 g5262560 4.00E−35 hypothetical protein 270 3 168 165 668 g10434856 5.00E−34 unnamed protein product 271 2 122 2 367 g12044553 8.00E−48 bA261P9.2 (putative novel protein similar to fly CG7340 and human putative aminopeptidase ZK353.6 in chromosome 3 (EC 3.4.11.-)) 271 2 122 2 367 g10432867 5.00E−47 unnamed protein product 271 2 122 2 367 g7299691 5.00E−42 BcDNA: LD41548 gene product (alt 1) 272 2 91 212 484 g872315 3.00E−35 40S ribosomal protein S12 272 2 91 212 484 g12842004 3.00E−35 putative 272 2 91 212 484 g12833134 3.00E−35 putative 273 3 225 3 677 g510552 1.00E−100 ribosomal protein L13 273 3 225 3 677 g12833027 1.00E−99 putative 273 3 225 3 677 g3869148 4.00E−98 robosomal protein L13 274 3 153 3 461 g825539 2.00E−84 MLC2 274 3 153 3 461 g1675396 2.00E−84 myosin light chain 2 274 3 153 3 461 g1637 2.00E−84 myosin light chain 2 type 2 275 2 296 176 1063 g12407387 1.00E−147 tripartite motif protein TRIM5 isoform delta 275 2 296 176 1063 g12407385 1.00E−47 tripartite motif protein TRIM5 isoform gamma 275 2 296 176 1063 g12407383 1.00E−147 tripartite motif protein TRIM5 isoform beta 276 1 175 22 546 g13752754 1.00E−26 zinc finger 1111 276 1 175 22 546 g14348588 5.00E−25 KRAB zinc finger protein 276 1 175 22 546 g12654015 4.00E−24 Similar to hypothetical protein FLJ10891 277 3 76 141 368 g9714522 5.00E−13 bA162G10.3 (zinc finger protein) 277 3 76 141 368 g5730194 5.00E−13 KRAB protein domain 277 3 76 141 368 g4589588 8.00E−13 KIAA0972 protein 278 3 146 624 1061 g12697318 5.00E−14 PBX4 protein 278 3 146 624 1061 g7160798 9.00E−13 pbxy homeodomain protein 278 3 146 624 1061 g634053 9.00E−13 PBX2 279 3 391 3 1175 g10439850 1.00E−116 unnamed protein product 279 3 391 3 1175 g9968290 1.00E−112 zinc finger protein 304 279 3 391 3 1175 g14249844 1.00E−111 Similar to hypothetical protein FLJ23233 280 3 80 156 395 g12052983 7.00E−15 hypothetical protein 280 3 80 156 395 g13277768 1.00E−11 zinc finger protein 93 280 3 80 156 395 g1184371 1.00E−11 zinc finger protein; Method: conceptual translation supplied by author 281 2 162 74 559 g6467206 8.00E−37 gonadotropin inducible transcription repressor-4 281 2 162 74 559 g9187356 2.00E−36 hypothetical protein, similar to (AB021644) GONADOTROPIN INDUCIBLE TRANSCRIPTION REPRESSOR-4 281 2 162 74 559 g220637 2.00E−36 zinc finger protein 282 2 164 50 541 g13752754 1.00E−28 zinc finger 1111 282 2 164 50 541 g14348588 5.00E−28 KRAB zinc finger protein 282 2 164 50 541 g12654015 3.00E−27 Similar to hypothetical protein FLJ10891 283 3 105 75 389 g12052732 2.00E−38 hypothetical protein 283 3 105 75 389 g3329372 9.00E−37 DNA-binding protein 283 3 105 75 389 g7959207 3.00E−34 KIAA1473 protein 284 1 123 289 657 g14042035 9.00E−64 unnamed protein product 284 1 123 289 657 g6224922 1.00E−41 BTB/POZ domain zinc finger factor HOF-S 284 1 123 289 657 g6063139 1.00E−41 BTB/POZ domain zinc finger factor HOF-L 285 1 174 199 720 g7022603 2.00E−20 unnamed protein product 285 1 174 199 720 g7022652 3.00E−10 unnamed protein product 285 1 174 199 720 g3283350 3.00E−08 calmodulin-binding protein SHA1 286 2 181 71 613 g13591714 4.00E−97 (AF343664) immunoglobulin superfamily receptor translocation associated protein 2c 286 2 181 71 613 g13591712 4.00E−97 (AF343663) immunoglobulin superfamily receptor translocation associated protein 2b 286 2 181 71 613 g13591710 4.00E−97 (AF343662) immunoglobulin superfamily receptor translocation associated protein 2a 287 1 91 64 336 g10047183 8.00E−48 KIAA1559 protein 287 1 91 64 336 g5080758 8.00E−25 BC331191_1 287 1 91 64 336 g456269 1.00E−21 zinc finger protein 30 288 1 188 226 789 g11999277 4.00E−45 solute carrier 288 1 188 226 789 g12845461 8.00E−34 putative 288 1 188 226 789 g10434874 2.00E−33 unnamed protein product 289 2 290 2 871 g14017771 1.00E−157 fibrillin3 289 2 290 2 871 g762831 1.00E−113 fibrillin 2 289 2 290 2 871 g4959652 1.00E−113 flbrillin-2 290 3 199 3 599 g3757719 1.00E−83 dJ422F24.1 (PUTATIVE novel protein similar to C. elegans C0202.5) 290 3 199 3 599 g12832288 5.00E−83 putative 290 3 199 3 599 g7294769 2.00E−38 CG6279 gene product 291 3 148 3 446 g13489168 5.00E−77 60S ribosomal protein L17 291 3 148 3 446 g13430182 3.00E−76 ribosomal protein L17 291 3 148 3 446 g14596111 2.00E−75 (AY042843) 60S ribosomal protein L17 292 1 92 37 312 g6002102 5.00E−39 Acyl-CoA binding protein (ACBP) 292 1 92 37 312 g1938236 3.00E−38 acyl-CoA-binding protein 292 1 92 37 312 g6002104 2.00E−37 Acyl-CoA binding protein (ACBP) 293 3 256 3 770 g5091520 1.00E−127 ESTs AU058081(E30812), AU058365(E50679), AU030138(E50679) correspond to a region of the predicted gene.; Similar to Spinacia oleracea mRNA for proteasome 37 kD subunit, (X96974) 293 3 256 3 770 g8671496 1.00E−127 alpha 3 subunit of 20S proteasome 293 3 256 3 770 g8096329 1.00E−127 ESTs AU058081(E3082), AU075427 (E30384) correspond to a region of the predicted gene, ˜Similar to Spinacia oleracea proteasome 27 kD subunit (P52427) 295 3 318 132 1085 g11602755 1.00E−37 zinc finger protein 295 3 318 132 1085 g12843135 6.00E−33 putative 295 3 318 132 1085 g13094151 3.00E−25 zinc finger protein hRit1 alpha 296 1 194 304 885 g12856559 1.00E−85 putative 296 1 194 304 885 g12856631 3.00E−85 putative 296 1 194 304 885 g12849896 3.00E−85 putative 297 1 469 1 1407 g9927838 0 unnamed protein product 297 1 469 1 1407 g10045028 0 unnamed protein product 297 1 469 1 1407 g10047295 1.00E−169 KIAA1610 protein 298 3 81 3 245 g13249093 5.00E−37 carbonic anhydrase XIII 298 3 81 3 245 g12845416 5.00E−37 putative 298 3 81 3 245 g65332 4.00E−22 carbonic anhydrase 299 1 452 1 1356 g11177164 0 polydom protein 299 1 452 1 1356 g12060830 1.00E−142 serologically defined breast cancer antigen NY-BR-38 299 1 452 1 1356 g7292728 1.00E−52 fw gene product 300 1 362 97 1182 g14594722 0 (AY037298) elongation of very long chain fatty acids protein 300 1 362 97 1182 g12044051 0 ELOVL4 300 1 362 97 1182 g12044043 0 ELOVL4 301 2 354 2 1063 g14272764 1.00E−146 unnamed protein product 301 2 354 2 1063 g561853 5.00E−28 megalin 301 2 354 2 1063 g1809240 7.00E−27 gp330 precursor 302 1 305 220 1134 g12483902 1.00E−83 zinc finger protein HIT-10 302 1 305 220 1134 g6002480 4.00E−49 BWSCR2 associated zinc-finger protein BAZ2 302 1 305 220 1134 g9963806 4.00E−47 zinc finger protein ZNF287 303 2 659 164 2140 g14587851 0 (AB050785) Graf2 303 2 659 164 2140 g13310137 0 PSGAP-m 303 2 659 164 2140 g13310135 0 PSGAP-s 304 3 390 102 1271 g13879442 1.00E−170 Similar to RIKEN cDNA 2310035M22 gene 304 3 390 102 1271 g12855490 1.00E−165 putative 304 3 390 102 1271 g12848905 1.00E−102 putative 305 2 294 2 883 g13898617 1.00E−142 serine/threonine protein kinase SSTK 305 2 294 2 883 g13540326 1.00E−142 serine/threonine kinase FKSG82 305 2 294 2 883 g13898619 1.00E−140 serine/threonine protein kinase SSTK 306 1 269 1 807 g14250138 1.00E−139 Similar to RIKEN cDNA 5730421E18 gene 306 1 269 1 807 g12856916 1.00E−120 putative 306 1 269 1 807 g12840367 1.00E−120 putative 307 3 270 393 1202 g10434082 1.00E−103 unnamed protein product 307 3 270 393 1202 g12052816 1.00E−102 hypothetical protein 307 3 270 393 1202 g297157 1.00E−74 rab17 308 3 358 150 1223 g12861800 1.00E−170 putative 308 3 358 150 1223 g3878713 5.00E−73 (Z46935) weak similarity with quinone oxidoreductase, contains similarity to Pfam domain: PF00107 (Zinc-binding dehydrogenases), Score = −80.6, E- value = 6.2e−06, N = 1˜cDNA EST yk164b4.5 comes from this gene˜ cDNA EST yk164b4.3 comes from this gene˜cDNA EST yk264f3.5 comes from this 308 3 358 150 1223 g2633069 2.00E−52 similar to quinone oxidoreductase 309 2 232 2 697 g12834244 1.00E−71 putative 309 2 232 2 697 g12833174 1.00E−71 putative 309 2 232 2 697 g13905260 1.00E−36 RIKEN cDNA 1300006C06 gene 310 3 184 3 554 g2335037 9.00E−67 Tim17 310 3 184 3 554 g4378524 2.00E−65 mitochondrial inner membrane translocase component Tlm17a 310 3 184 3 554 g12833600 2.00E−65 putative 311 1 206 46 663 g12314268 4.00E−82 dJ14N1.2 (novel S-100/ICaBP type calcium binding domain protein, similar to trichohyalin) 311 1 206 46 663 g553621 3.00E−14 profilaggrin 311 1 206 46 663 g12314267 3.00E−14 dJ14N1.1.1 (profilaggrin 5′ end) 312 2 301 59 961 g12314195 1.00E−171 bA255A11.3 (novel protein similar to KIAA1074) 312 2 301 59 961 g12314164 1.00E−134 bA526D8.2 (novel protein similar to KIAA1074) 312 2 301 59 961 g12053099 4.00E−95 hypothetical protein 313 1 156 70 537 g6692607 2.00E−65 MGA protein 313 1 156 70 537 g5931585 1.00E−44 T-box family member; T-box domain 313 1 156 70 537 g4049463 4.00E−16 transcription factor TBX6 314 1 279 340 1176 g12854977 1.00E−123 putative 314 1 279 340 1176 g7267246 1.00E−41 putative adenosine deaminase 314 1 279 340 1176 g7299138 2.00E−39 CG11994 gene product 315 1 329 181 1167 g4582324 0 dJ708F5.1 (PUTATIVE novel Collagen alpha 1 LIKE protein) 315 1 329 181 1167 g12052774 0 hypothetical protein 315 1 329 181 1167 g2326442 1.00E−38 collagen type XII alpha 1 chain 316 3 757 3 2273 g8896164 0 kinesin-like protein GAKIN 316 3 757 3 2273 g10697238 0 KIF13A 316 3 757 3 2273 g12054032 0 KINESIN-13A2 317 1 329 1 987 g14595658 8.00E−97 (AF387815) LIM protein prickle 317 1 329 1 987 g9229890 3.00E−84 prickle 2 317 1 329 1 987 g9229888 3.00E−83 prickle 1 318 1 494 1 1482 g1763096 0 glutamate pyruvate transaminase 318 1 494 1 1482 g467528 0 alanine aminotransferase 318 1 494 1 1482 g1507680 0 alanine aminotransferase 319 1 156 400 867 g5912051 2.00E−30 hypothetical protein 319 1 156 400 867 g14278937 2.00E−30 calmin 319 1 156 400 867 g10437695 2.00E−30 unnamed protein product 320 1 128 118 501 g7294107 4.00E−44 CG4638 gene product 320 1 128 118 501 g3169065 3.00E−40 elongation factor 2-like protein 320 1 128 118 501 g1302132 4.00E−38 ORF YNL163c 321 1 197 151 741 g13185203 2.00E−21 unnamed protein product 321 1 197 151 741 g2463632 3.00E−14 monocarboxylate transporter homologue MCT6 321 1 197 151 741 g6103363 3.00E−13 monocarboxylate transporter MCT3 322 1 560 1 1680 g4240293 1.00E−141 KIAA0902 protein 322 1 560 1 1680 g4151807 1.00E−141 membrane-associated guanylate kinase- interacting protein 2 Maguin-2 322 1 560 1 1680 g4151805 1.00E−141 membrane-associated guanylate kinase- interacting protein 1 Maguin-1 323 2 163 2 490 g10172680 3.00E−06 stage V sporulation protein C (peptidyl-tRNA hydrolase) 323 2 163 2 490 g1001232 4.00E−06 (D64003) peptidyl-tRNA hydrolase 323 2 163 2 490 g2983032 1.00E−05 peptidyl-tRNA hydrolase 324 2 197 2 592 g9295345 2.00E−67 HSKM-B 324 2 197 2 592 g12834773 5.00E−19 putative 324 2 197 2 592 g5870834 3.00E−17 skm-BOP2 325 3 520 3 1562 g8655678 1.00E−139 hypothetical protein 325 3 520 3 1562 g12382779 1.00E−59 zinc transporter 1 325 3 520 3 1562 g577843 2.00E−59 ZnT-1 326 1 772 640 2955 g13358642 0 hypothetical protein 326 1 772 640 2955 g10435064 0 unnamed protein product 326 1 772 640 2955 g10434826 0 unnamed protein product 327 3 702 153 2258 g7264026 0 dJ876B10.2 (novel protein (ortholog of rat EXO84)) 327 3 702 153 2258 g2827164 0 exo84 327 3 702 153 2258 g7301432 2.00E−38 CG6095 gene product 328 3 255 609 1373 g13383265 1.00E−106 actin related protein 328 3 255 609 1373 g13938319 1.00E−105 Unknown (protein for MGC: 15664) 328 3 255 609 1373 g12840619 9.00E−72 putative 330 2 178 203 736 g10435210 2.00E−76 unnamed protein product 330 2 178 203 736 g14598968 3.00E−58 (AX179297) 21615 ADH 330 2 178 203 736 g8895083 3.00E−58 oxidoreductase UCPA 331 1 217 1624 2274 g8655648 1.00E−108 hypothetical protein 331 1 217 1624 2274 g12803319 1.00E−108 Unknown (protein for MGC: 3090) 331 1 217 1624 2274 g10047337 1.00E−108 KIAA1630 protein 332 1 191 823 1395 g9651711 4.00E−72 arsenite inducible RNA associated protein 332 1 191 823 1395 g12835478 3.00E−53 putative 332 1 191 823 1395 g7295806 6.00E−45 CG12795 gene product 333 2 252 1223 1978 g12856598 6.00E−93 putative 333 2 252 1223 1978 g14042913 2.00E−19 unnamed protein product 333 2 252 1223 1978 g14424618 9.00E−19 hypothetical protein MGC2628 334 2 502 305 1810 g12845866 1.00E−131 putative 334 2 502 305 1810 g13477235 4.00E−80 Similar to RIKEN cDNA 0610037N03 gene 334 2 502 305 1810 g12833017 6.00E−22 putative 335 2 369 2 1108 g12856270 1.00E−165 putative 335 2 369 2 1108 g6682873 1.00E−119 reduced expression in cancer 335 2 369 2 1108 g7230612 1.00E−116 small rec 337 2 332 2 997 g8886025 1.00E−166 collapsin response mediator protein-5 337 2 332 2 997 g8671168 1.00E−166 hypothetical protein 337 2 332 2 997 g13259169 1.00E−166 phosphoprotein ULIP6 338 1 215 73 717 g12652727 1.00E−125 Unknown (protein for IMAGE: 3352566) 338 1 215 73 717 g488555 2.00E−67 zinc finger protein ZNF135 338 1 215 73 717 g8050899 6.00E−65 ZNF180 339 3 364 3 1094 g9758769 1.00E−64 11-beta-hydroxysteroid dehydrogenase-like 339 3 364 3 1094 g8777393 1.00E−64 11-beta-hydroxysteroid dehydrogenase-like 339 3 364 3 1094 g8777400 1.00E−54 contains similarity to oxidoreductase˜ gene_id: MFB16.17 340 3 229 21 707 g12052959 1.00E−130 hypothetical protein 340 3 229 21 707 g14336767 1.00E−128 similar to homoprotocatechuate catabolism bifunctional isomerase/decarboxylase 340 3 229 21 707 g7670464 1.00E−115 unnamed protein product 341 1 164 235 726 g2286123 8.00E−47 testis specific DNAj-homolog 341 1 164 235 726 g12838392 8.00E−47 putative 341 1 164 235 726 g12838396 4.00E−46 putative 342 1 131 199 591 g12804323 5.00E−60 Unknown (protein for MGC: 4054) 342 1 131 199 591 g3264773 5.00E−32 zinc-finger protein-37; ZFP-37 342 1 131 199 591 g10440398 5.00E−32 FLJ00032 protein 343 2 406 701 1918 g12697482 1.00E−121 dJ583P15.7.2 (novel zinc finger protein similar to rat RIN ZF) 343 2 406 701 1918 g12855580 1.00E−81 putative 343 2 406 701 1918 g12847599 7.00E−78 putative 344 3 219 3 659 g6091722 3.00E−51 putative ribosomal protein L13 344 3 219 3 659 g6650751 2.00E−49 ribosomal protein I 344 3 219 3 659 g2984157 4.00E−28 ribosomal protein L13 345 2 134 95 496 g14042747 4.00E−63 unnamed protein product 345 2 134 95 496 g10440516 4.00E−63 FLJ00106 protein 345 2 134 95 496 g10445215 7.00E−62 PDZ-LIM protein mystique 346 3 174 3 524 g11527997 1.00E−112 NOTCH2 protein 346 3 174 3 524 g11275978 1.00E−112 NOTCH 2 346 3 174 3 524 g287990 1.00E−112 Motch B 347 1 306 202 1119 g14024759 4.00E−32 aldehyde dehydrogenase 347 1 306 202 1119 g13162101 3.00E−28 putative aldehyde dehydrogenase 347 1 306 202 1119 g14025513 1.00E−23 succinate-semialdehyde dehydrogenase 348 3 283 819 1667 g10438978 1.00E−156 unnamed protein product 348 3 283 819 1667 g13358630 1.00E−155 hypothetical protein 348 3 283 819 1667 g9280094 1.00E−36 unnamed protein product 349 3 188 123 686 g4126809 5.00E−88 glyoxalase I 349 3 188 123 686 g1808684 3.00E−84 hypothetical protein 349 3 188 123 686 g2213425 8.00E−81 hypothetical protein 350 1 176 1 528 g57469 2.00E−98 vasopressin 350 1 176 1 528 g4469315 2.00E−98 vasopressin precursor 350 1 176 1 528 g207674 3.00E−96 vasopressin/neurophysin precursor 351 1 52 253 408 g3790135 3.00E−18 dJ191N21.3 (proteasome subunit HC5) 351 1 52 253 408 g220026 3.00E−18 proteasome subunit C5 351 1 52 253 408 g1698584 3.00E−18 proteasome beta-subunit C5 352 3 190 3 572 g205662 5.00E−86 nucleoside diphosphate kinase 352 3 190 3 572 g206580 4.00E−85 RBL-NDP kinase 18 kDa subunit (p18) 352 3 190 3 572 g53354 5.00E−85 nucleoside diphosphate kinase B 353 3 135 546 950 g9368839 1.00E−37 hypothetical protein 353 3 135 546 950 g57690 9.00E−29 ribosomal protein L23a 353 3 135 546 950 g404015 9.00E−29 ribosomal protein L23a 354 1 517 1 1551 g13161184 0 cytochrome P450 2S1 354 1 517 1 1551 g14042396 0 unnamed protein product 354 1 517 1 1551 g12836063 0 putative 355 2 135 203 607 g7677318 5.00E−55 aldehyde reductase 355 2 135 203 607 g12848322 5.00E−55 putative 355 2 135 203 607 g12848318 5.00E−55 putative 356 3 77 42 272 g3851089 1.00E−24 guanine nucleotide binding protein gamma 5 356 3 77 42 272 g3329380 1.00E−24 G protein gamma 5 subunit 356 3 77 42 272 g204241 1.00E−24 G protein gamma-5 subunit 357 3 110 96 425 g7340072 4.00E−15 40S ribosomal protein S15A 357 3 110 96 425 g495273 4.00E−15 ribosomal protein S15a 357 3 110 96 425 g12859337 4.00E−15 putative 358 1 485 1 1455 g10436300 0 unnamed protein product 358 1 485 1 1455 g10433852 0 unnamed protein product 358 1 485 1 1455 g9280029 0 unnamed protein product 360 1 143 1 429 g63466 2.00E−56 histone H2A 360 1 143 1 429 g6094631 2.00E−56 histone H2A.F 360 1 143 1 429 g3420799 2.00E−56 histone H2A.F/Z variant 361 3 81 159 401 g10437078 4.00E−34 unnamed protein product 361 3 81 159 401 g12859774 600E−33 putative 361 3 81 159 401 g12857408 6.00E−33 putative 362 3 543 834 2462 g12849316 4.00E−87 putative 362 3 543 834 2462 g6164628 3.00E−86 SH3 and PX domain-containing protein SH3PX1 362 3 543 834 2462 g5410249 3.00E−86 SDP1 protein 363 1 185 1 555 g12836716 1.00E−103 putative 363 1 185 1 555 g12834312 1.00E−103 putative 363 1 185 1 555 g12832330 1.00E−103 putative 364 3 156 177 644 g14456629 1.00E−31 dJ54B20.2 (novel KRAB box containing C2H2 type zinc finger protein) 364 3 156 177 644 g4589588 9.00E−27 KIAA0972 protein 364 3 156 177 644 g3970712 3.00E−23 zinc finger protein 10 365 1 183 235 783 g12248382 7.00E−31 SEMB 365 1 183 235 783 g854326 7.00E−29 semaphorin B 365 1 183 235 783 g1110599 1.00E−14 semaphorin homolog = M-Sema F (mice, neonatal brain, Peptide, 834 aa) 366 1 416 1 1248 g13543419 1.00E−161 Similar to zinc finger protein 304 366 1 416 1 1248 g7020745 5.00E−53 unnamed protein product 366 1 416 1 1248 g12652759 5.00E−53 hypothetical protein FLJ20557 367 2 258 455 1228 g1174187 2.00E−94 purine nucleotide binding protein 367 2 258 455 1228 g193444 8.00E−88 guanylate binding protein 367 2 258 455 1228 g829177 1.00E−68 guanylate binding protein isoform II 368 3 68 270 473 g14586963 7.00E−10 (AF362574) M75 368 3 68 270 473 g57115 7.00E−10 ribosomal protein L31 (AA 1-125) 368 3 68 270 473 g36130 7.00E−10 ribosomal protein L31 (AA 1-125) 371 1 122 568 933 g10435150 2.00E−39 unnamed protein product 371 1 122 568 933 g4982195 2.00E−16 lepA protein 371 1 122 568 933 g2984041 6.00E−16 G-protein LepA 372 3 111 3 335 g13752754 3.00E−15 zinc finger 1111 372 3 111 3 335 g7023216 2.00E−14 unnamed protein product 372 3 111 3 335 g14348588 2.00E−14 KRAB zinc finger protein 373 3 1281 36 3878 g157409 2.00E−95 fat protein 373 3 1281 36 3878 g7295732 3.00E−94 ft gene product 373 3 1281 36 3878 g10727403 2.00E−93 ds gene product 374 3 164 3 494 g9759463 2.00E−60 40S ribosomal protein S19 374 3 164 3 494 g6513924 4.00E−60 putative 40S ribosomal protein S19 374 3 164 3 494 g13878029 4.00E−60 putative 40S ribosomal protein S19 375 3 365 750 1844 g55628 0 reading frame (preproalbumin) 375 3 365 750 1844 g3647327 0 serum albumin 375 3 365 750 1844 g12845183 0 putative 376 1 96 184 471 g12853416 5.00E−25 putative 376 1 96 184 471 g13529497 8.00E−23 Unknown (protein for MGC: 6652) 376 1 96 184 471 g4589588 5.00E−22 KIAA0972 protein 377 2 106 125 442 g14042293 3.00E−37 unnamed protein product 377 2 106 125 442 g12052983 3.00E−37 hypothetical protein 377 2 106 125 442 g14043841 7.00E−34 Unknown (protein for MGC: 14429) 378 2 119 2 358 g57710 2.00E−31 ribosomal phosphoprotein P1 (AA 1-114) 378 2 119 2 358 g190234 2.00E−31 acidic ribosomal phosphoprotein (P1) 378 2 119 2 358 g14043204 2.00E−31 ribosomal protein, large, P1 380 2 282 2 847 g10440398 8.00E−93 FLJ00032 protein 380 2 282 2 847 g10047297 8.00E−93 KIAA1611 protein 380 2 282 2 847 g10436789 6.00E−92 unnamed protein product 381 2 47 287 427 g7290056 2.00E−10 EG: 118B3.2 gene product (alt 2) 381 2 47 287 427 g5901822 2.00E−10 EG: 118B3.2 381 2 47 287 427 g3645991 2.00E−10 /prediction = (method: ““genefinder””, version: ““084””, score: ““128.32””)˜/ prediction = (method: ““genscan””, version: ““1.0””)˜/ match = (desc: ““KIAA0376 PROTEIN (FRAGMENT)””, species: ““HOMO SAPIENS (HUMAN)””, ranges: (query:15779 . . . 16030, target: SPTREMBL::O15081:314 . . . 231, score: ““229.00””), (query:14786 . . . 15736, target: SPTREMBL::O15081: 650 . . . 334, score: ““319.00””), (query: 13868 . . . 13960, target: SPTREMBL::O15081: 884 . . . 854, score:““156.00””)), method: ““blastx””, version: ““1.4.9””)˜/ match = (desc: ““SPECTRIN BETA CHAIN, ERYTHROCYTE””, species: ““HOMO SAPIENS (HUMAN) ””, ranges: (query: 13748 . . . 13954, target: SWISS-PROT::P11277: 242 . . . 174, score: ““201.00””)), method:““blastx””, version: ““1.4.9””)˜/ match = (desc: ““ GH04661.5prime GH Drosophila melanogaster head pOT2 Drosophila melanogaster cDNA clone GH046615 prime, mRNA sequence””, species: ““Drosophila melanogaster (fruit fly)””, ranges: (query: 22139 . . . 22499, target: EMBL::AI064293: 361 . . . 1, score: ““1796.00””)), method: ““blastn””, version: ““1.4.9””)˜/ match = (desc: ““GH05563.5prime GH Drosophila melanogaster head pOT2 Drosophila melanogaster cDNA clone GH05563 383 1 280 16 855 g14456629 9.00E−90 dJ54B20.2 (novel KRAB box containing C2H2 type zinc finger protein) 383 1 280 16 855 g3378094 3.00E−72 KRAB domain zinc finger protein 383 1 280 16 855 g1020145 1.00E−71 DNA binding protein 384 3 264 3 794 g6807587 1.00E−124 hypothetical protein 384 3 264 3 794 g5931821 1.00E−124 dJ228H13.3 (zinc finger protein) 384 3 264 3 794 g488555 1.00E−96 zinc finger protein ZNF135 385 3 561 135 1817 g10954044 0 KRAB zinc finger protein ZFQR 385 3 561 135 1817 g10442700 0 zinc-finger protein ZBRK1 385 3 561 135 1817 g10435411 0 unnamed protein product 386 2 288 206 1069 g10439850 4.00E−70 unnamed protein product 386 2 288 206 1069 g4894364 6.00E−64 zinc finger protein 3 386 2 288 206 1069 g12655165 6.00E−64 zinc finger protein 256 387 3 476 171 1598 g14042538 0 unnamed protein product 387 3 476 171 1598 g10438630 0 unnamed protein product 387 3 476 171 1598 g13096919 0 Similar to zinc finger protein 135 (clone pHZ-17) 389 3 60 78 257 g5262560 5.00E−07 hypothetical protein 389 3 60 78 257 g10434856 5.00E−07 unnamed protein product 389 3 60 78 257 g13623354 6.00E−07 Similar to zinc finger protein 136 (clone pHZ-20) 390 2 355 254 1318 g10047183 1.00E−94 KIAA1559 protein 390 2 355 254 1318 g13676461 6.00E−81 hypothetical protein 390 2 355 254 1318 g4589566 1.00E−80 KIAA0961 protein 391 1 101 112 414 g13937999 3.00E−48 Similar to DNA-binding protein 391 1 101 112 414 g3329372 1.00E−34 DNA-binding protein 391 1 101 112 414 g12052732 3.00E−34 hypothetical protein 392 3 326 3 980 g14017921 0 KIAA1852 protein 392 3 326 3 980 g8050899 1.00E−133 ZNF180 392 3 326 3 980 g6409345 1.00E−133 zinc finger protein ZNF180 393 3 263 792 1580 g5441615 1.00E−96 zinc finger protein 393 3 263 792 1580 g498721 1.00E−94 zinc finger protein 393 3 263 792 1580 g8099348 2.00E−93 zinc finger protein 394 3 121 372 734 g10439850 3.00E−18 unnamed protein product 394 3 121 372 734 g14249844 7.00E−18 Similar to hypothetical protein FLJ23233 394 3 121 372 734 g2689441 4.00E−13 F18547_1 395 2 298 2 895 g10437560 0 unnamed protein product 395 2 298 2 895 g10047305 0 KIAA1615 protein 395 2 298 2 895 g498721 4.00E−86 zinc finger protein 396 1 287 220 1080 g14042550 3.00E−94 unnamed protein product 396 1 287 220 1080 g13937909 3.00E−94 Similar to KIAA0961 protein 396 1 287 220 1080 g10047183 5.00E−78 KIAA1559 protein 397 1 281 277 1119 g3540177 1.00E−123 F23269_2 397 1 281 277 1119 g5080758 1.00E−120 BC331191_1 397 1 281 277 1119 g12855931 5.00E−73 putative 398 1 263 1 789 g10434650 4.00E−88 unnamed protein product 398 1 263 1 789 g13623217 2.00E−40 Similar to hypothetical protein FLJ12895 398 1 263 1 789 g7020855 6.00E−27 unnamed protein product 399 2 646 200 2137 g14042373 0 unnamed protein product 399 2 646 200 2137 g498152 0 ha0946 protein is Kruppel-related. 399 2 646 200 2137 g7243633 0 RB-associated KRAB repressor 400 2 199 140 736 g204123 5.00E−89 ferritin light chain 400 2 199 140 736 g204133 6.00E−89 ferritin light chain 400 2 199 140 736 g193275 6.00E−89 ferritin light chain 401 1 210 25 654 g9651704 4.00E−79 carboxypeptidase B precursor 401 1 210 25 654 g6013463 8.00E−61 carboxypeptidase homolog 401 1 210 25 654 g203295 8.00E−61 carboxypeptidase B 402 2 390 2 1171 g13365901 0 hypothetical protein 402 2 390 2 1171 g2104689 1.00E−126 alpha glucosidase II, alpha subunit 402 2 390 2 1171 g1890664 1.00E−126 glucosidase II 403 3 43 348 476 g12052884 3.00E−06 hypothetical protein 403 3 43 348 476 g7023332 4.00E−06 unnamed protein product 403 3 43 348 476 g183002 6.00E−05 guanylate binding protein isoform I 404 1 406 1 1218 g12053281 0 hypothetical protein 404 1 406 1 1218 g12836135 1.00E−167 putative 404 1 406 1 1218 g3043598 2.00E−64 KIAA0537 protein 405 1 90 1 270 g7981261 4.00E−33 dJ50O24.4 (novel protein with DHHC zinc finger domain) 405 1 90 1 270 g14035816 4.00E−33 unnamed protein product 405 1 90 1 270 g12224992 4.00E−33 hypothetical protein 407 2 192 44 619 g7297667 1.00E−30 CG5022 gene product 407 2 192 44 619 g2224617 4.00E−30 KIAA0338 407 2 192 44 619 g13277297 4.00E−30 bA234K24.1.2 (Erythrocyte membrane protein band 4.1-like 1 protein (KIAA0338) Isoform 2) 408 1 183 28 576 g12314083 9.00E−94 dJ1007G16.5 (novel high-mobility group (nonhistone chromosomal) protein 2 (HMG2) like protein) 408 1 183 28 576 g12838247 4.00E−67 putative 408 1 183 28 576 g1304193 9.00E−35 HMG2 409 3 163 3 491 g12697320 8.00E−51 Pbx4 protein 409 3 163 3 491 g7160800 3.00E−50 Pbx4/Lazarus homeodomain protein 409 3 163 3 491 g5679283 3.00E−50 Pbx4 homeodomain protein 410 3 186 198 755 g12840673 2.00E−48 putative 410 3 186 198 755 g607003 4.00E−18 beta transducin-like protein 410 3 186 198 755 g3878300 1.00E−14 predicted using Genefinder˜Similarity to C.elegans Guanine nucleotide binding protein (WP: C14B1.4), contains similarity to Pfam domain: PF00400 (WD domain, G-beta repeat), Score = 196.1, E-value = 1.8e−55, N = 7˜cDNA EST yk567g12.3 comes from this gene˜cDNA EST yk567g12.5 comes from this gene 411 1 134 286 687 g11342541 2.00E−67 putative white family ATP-binding cassette transporter 411 1 134 286 687 g9665220 3.00E−50 ATP-binding cassette transporter, sub-family G member 1 411 1 134 286 687 g7768742 3.00E−50 white protein homolog (ATP-binding cassette transporter 8) 412 2 97 35 325 g57175 1.00E−37 S-100 protein 412 2 97 35 325 g206825 1.00E−37 S100 protein 412 2 97 35 325 g404769 2.00E−37 S100 beta protein 413 1 181 1 543 g13543071 9.00E−64 RIKEN cDNA 1500031N16 gene 413 1 181 1 543 g12837801 9.00E−64 putative 413 1 181 1 543 g12832973 5.00E−60 putative 414 3 258 3 776 g12856949 4.00E−98 putative 414 3 258 3 776 g12653785 3.00E−97 Unknown (protein for IMAGE: 3349601) 414 3 258 3 776 g12845723 4.00E−94 putative 415 2 169 2 508 g7259240 1.00E-79 unnamed protein product 415 2 169 2 508 g12845457 1.00E−79 putative 415 2 169 2 508 g12834293 1.00E−79 putative 416 1 177 310 840 g9502403 5.00E−06 Hypothetical zinc finger-like protein 417 1 81 451 693 g14042550 6.00E−27 unnamed protein product 417 1 81 451 693 g13937909 6.00E−27 Similar to KIAA0961 protein 417 1 81 451 693 g487787 3.00E−23 zinc finger protein ZNF140 418 2 94 329 610 g13752754 7.00E−18 zinc finger 1111 418 2 94 329 610 g14348588 1.00E−16 KRAB zinc finger protein 418 2 94 329 610 g12654015 1.00E−16 Similar to hypothetical protein FLJ10891 419 3 165 3 497 g12856090 2.00E−51 putative 419 3 165 3 497 g12854104 2.00E-51 putative 419 3 165 3 497 g4678718 4.00E−43 dJ2013.1 (brain mitochondrial carrier protein-1 (BMCP1)) 420 3 352 111 1166 g13444976 4.00E−36 unnamed protein product 420 3 352 111 1166 g12309630 4.00E−36 bA438B23.1 (neuronal leucine-rich repeat protein) 420 3 352 111 1166 g9651089 8.00E−34 hypothetical protein 421 2 113 2 340 g14164613 3.00E−27 sialic acid binding immunoglobulin-like lectin 10 421 2 113 2 340 g13991167 6.00E−16 sialic acid-binding immunoglobulin-like lectin-like long splice variant 421 2 113 2 340 g13991166 6.00E−16 sialic acid-binding immunoglobulin-like lectin-like short splice variant 422 2 100 101 400 g12052732 1.00E−38 hypothetical protein 422 2 100 101 400 g3329372 8.00E−37 DNA-binding protein 422 2 100 101 400 g7959207 2.00E−34 KIAA1473 protein 423 1 117 1 351 g7959207 800E−39 KIAA1473 protein 423 1 117 1 351 g3342002 2.00E−36 hematopoietic cell derived zinc finger protein 423 1 117 1 351 g186774 5.00E−35 zinc finger protein 424 2 250 2 751 g14042850 2.00E−50 unnamed protein product 424 2 250 2 751 g12052983 8.00E−37 hypothetical protein 424 2 250 2 751 g14042293 1.00E−36 unnamed protein product 425 1 199 1 597 g10437560 1.00E−105 unnamed protein product 425 1 199 1 597 g10047305 1.00E−105 KIAA1615 protein 425 1 199 1 597 g13436440 2.00E−77 Unknown (protein for MGC: 4400) 426 3 166 3 500 g14017833 3.00E−86 KIAA1808 protein 426 3 166 3 500 g4240175 6.00E−24 KIAA0843 protein 426 3 166 3 500 g505094 5.00E−21 similar to an actin bundling protein, dematn. 427 1 157 1168 1638 g14042421 4.00E−11 unnamed protein product 427 1 157 1168 1638 g14017937 4.00E−11 KIAA1860 protein 427 1 157 1168 1638 g13366084 4.00E−11 MAP/microtubule affinity-regulating kinase like 1 429 3 200 3 602 g9651099 1.00E−118 hypothetical protein 429 3 200 3 602 g881564 1.00E−55 ZNF157 429 3 200 3 602 g453466 5.00E−55 zinc finger protein 430 2 173 2 520 g11990770 2.00E−67 bA534G20.1.1 (novel protein similar to Lysozyme C-1 (1,4-beta-N- acylmuramidase C, EC 3.2.1.17) (isoform 1)) 430 2 173 2 520 g11990771 1.00E−56 bA534G20.1.2 (novel protein similar to Lysozyme C-1 (1,4-beta-N- acylmuramidase C, EC 3.2.1.17) (isoform 2)) 430 2 173 2 520 g12839824 3.00E−49 putative 431 1 181 76 618 g13591714 4.00E−97 (AF343664) immunoglobulin superfamily receptor translocation associated protein 2c 431 1 181 76 618 g13591712 4.00E−97 (AF343663) immunoglobulin superfamily receptor translocation associated protein 2b 431 1 181 76 618 g13591710 4.00E−97 (AF343662) immunoglobulin superfamily receptor translocation associated protein 2a 433 1 157 22 492 g7268562 7.00E−54 ribosomal protein L32-like protein 433 1 157 22 492 g5816996 7.00E−54 ribosomal protein L32-like protein 433 1 157 22 492 g13899057 2.00E−53 ribosomal protein L32 434 1 182 157 702 g12855141 5.00E−89 putative 434 1 182 157 702 g12852338 5.00E−89 putative 434 1 182 157 702 g12849745 5.00E−89 putative 435 2 134 2 403 g2624328 2.00E−44 OsGRP2 435 2 134 2 403 g2366750 2.00E−34 RNA binding protein 435 2 134 2 403 g7268089 8.00E−34 glycine-rich RNA-binding protein AtGRP2-like 436 2 148 731 1174 g13397122 1.00E−58 unnamed protein product 436 2 148 731 1174 g12654715 1.00E−58 Similar to glucose regulated protein, 58 kDa 436 2 148 731 1174 g10728195 3.00E−15 CG1837 gene product 437 2 296 2 889 g12597312 1.00E−149 tRNA-guanine transglycosylase 437 2 296 2 889 g12597314 1.00E−137 tRNA-guanine transglycosylase 437 2 296 2 889 g7415812 1.00E−135 tRNA-guanine transglycosylase 438 3 169 9 515 g12406772 4.00E−52 unnamed protein product 438 3 169 9 515 g12406688 4.00E−52 unnamed protein product 438 3 169 9 515 g7299372 4.00E−29 CG6567 gene product 439 2 170 200 709 g14133251 3.00E−93 KIAA1479 protein 439 2 170 200 709 g2623162 7.00E−39 semaphorin VIa 439 2 170 200 709 g11093909 7.00E−39 axon guidance signal SEMA6A1 440 2 841 2 2524 g11177164 0 polydom protein 440 2 841 2 2524 g12060830 1.00E−155 serologically defined breast cancer antigen NY-BR-38 440 2 841 2 2524 g14198157 4.00E−83 polydomain protein 441 1 271 70 882 g13898617 1.00E−142 serine/threonine protein kinase SSTK 441 1 271 70 882 g13540326 1.00E−142 serine/threonine kinase FKSG82 441 1 271 70 882 g13898619 1.00E−140 serine/threonine protein kinase SSTK 442 2 311 743 1675 g8979743 1.00E−160 Band4.1-like5 protein 442 2 311 743 1675 g13278193 1.00E−153 Similar to EHM2 gene 442 2 311 743 1675 g10434740 1.00E−140 unnamed protein product 443 2 529 416 2002 g12834087 1.00E−155 putative 443 2 529 416 2002 g2463628 6.00E−46 putative monocarboxylate transporter 443 2 529 416 2002 g7328162 1.00E−40 hypothetical protein 444 1 335 4 1008 g13159480 1.00E−128 Translation may initiate at the ATG codon at nucleotides 40-42 or the ATG at nucleotides 43-45 444 1 335 4 1008 g9229906 5.00E−35 fibrinogen-like protein 444 1 335 4 1008 g387156 8.00E−33 fibrinogen-like protein 445 1 329 196 1182 g4582324 0 dJ708F5.1 (PUTATIVE novel Collagen alpha 1 LIKE protein) 445 1 329 196 1182 g12052774 0 hypothetical protein 445 1 329 196 1182 g2326442 1.00E−38 collagen type XII alpha 1 chain 446 2 395 110 1294 g12642596 0 nuclear receptor co-repressor/ HDAC3 complex subunit TBLR1 446 2 395 110 1294 g10434648 0 unnamed protein product 446 2 395 110 1294 g12006104 0 IRA1 447 1 163 1 489 g12858551 7.00E−67 putative 447 1 163 1 489 g12805285 7.00E−67 Similar to ribosomal protein S27a 447 1 163 1 489 g1050756 7.00E−67 fusion protein: ubiquitin (bases 43_513); ribosomal protein S27a (bases 217_532) 448 3 78 330 563 g8699209 5.00E−06 cyclophilin A 448 3 78 330 563 g50621 5.00E−06 cyclophilin (AA 1-164) 448 3 78 330 563 g49496 5.00E−06 cyclophilin (AA 1-164) 449 1 314 277 1218 g12844770 1.00E−130 putative 449 1 314 277 1218 g12861366 1.00E−127 putative 449 1 314 277 1218 g12857383 7.00E−50 putative 450 1 130 181 570 g2843171 4.00E−06 zinc finger protein 450 1 130 181 570 g5817149 5.00E−06 hypothetical protein 450 1 130 181 570 g10434142 5.00E−06 unnamed protein product 451 1 176 697 1224 g13383265 1.00E−63 actin related protein 451 1 176 697 1224 g13938319 3.00E−62 Unknown (protein for MGC: 15664) 451 1 176 697 1224 g12840619 2.00E−51 putative 452 3 671 3 2015 g12698057 1.00E−168 KIAA1756 protein 452 3 671 3 2015 g1177322 1.00E−124 CPG2 protein 452 3 671 3 2015 g10728577 1.00E−82 Msp-300 gene product 453 3 293 3 881 g4235148 8.00E−85 BC41195_1 453 3 293 3 881 g14165525 7.00E−71 Similar to CG8500 gene product 453 3 293 3 881 g14388336 2.00E−70 hypothetical protein 455 1 253 478 1236 g14424576 1.00E−118 hypothetical protein FLJ21963 455 1 253 478 1236 g10438188 1.00E−118 unnamed protein product 455 1 253 478 1236 g14025162 3.00E−57 acetyl-coa synthetase 457 1 125 529 903 g12859335 1.00E−26 putative 457 1 125 529 903 g12858578 1.00E−26 putative 457 1 125 529 903 g12843085 6.00E−21 putative 458 1 394 577 1758 g14533376 1.00E−148 (AX151207) unnamed protein product 458 1 394 577 1758 g11762100 1.00E−144 myo-inositol 1-phosphate synthase 458 1 394 577 1758 g3108053 1.00E−144 myo-inositol 1-phosphate synthase; INO1 459 3 149 1137 1583 g12053149 2.00E−39 hypothetical protein 460 2 323 122 1090 g7297059 3.00E−06 CG9117 gene product 461 3 200 387 986 g13365897 1.00E−82 hypothetical protein 461 3 200 387 986 g2636109 2.00E−24 similar to metabolite transport protein 461 3 200 387 986 g1894771 2.00E−24 product highly similar to metabolite transport proteins 462 2 406 701 1918 g12697482 1.00E−121 dJ583P15.7.2 (novel zinc finger protein similar to rat RIN ZF) 462 2 406 701 1918 g12855580 1.00E−81 putative 462 2 406 701 1918 g12847599 7.00E−78 putative 463 3 181 102 644 g13879442 2.00E−78 Similar to RIKEN cDNA 2310035M22 gene 463 3 181 102 644 g12848905 2.00E−78 putative 463 3 181 102 644 g12855490 1.00E−73 putative 464 3 137 69 479 g11231085 7.00E−29 hypothetical protein 464 3 137 69 479 g10998425 6.00E−09 NORPEG-like protein 464 3 137 69 479 g10937641 6.00E−09 ankycorbin 465 2 278 218 1051 g12861800 1.00E−111 putative 465 2 278 218 1051 g3878713 2.00E−38 (Z46935) weak similarity with quinone oxidoreductase, contains similarity to Pfam domain: PF00107 (Zinc-binding dehydrogenases), Score = −80.6, E- value = 6.2e−06, N = 1˜cDNA EST yk164b4.5 comes from this gene˜cDNA EST yk164b4.3 comes from this gene˜ cDNA EST yk264f3.5 comes from this 465 2 278 218 1051 g9948219 4.00E−36 conserved hypothetical protein 467 1 142 118 543 g4559318 4.00E−17 BC273239_1 467 1 142 118 543 g186774 9.00E−17 zinc finger protein 467 1 142 118 543 g1017722 9.00E−17 repressor transcriptional factor 468 3 126 78 455 g9963804 5.00E−47 zinc finger protein ZNF286 468 3 126 78 455 g14017965 5.00E−47 KIAA1874 protein 468 3 126 78 455 g5640017 2.00E−46 zinc finger protein ZFP113 469 3 246 228 965 g13676461 1.00E−45 hypothetical protein 469 3 246 228 965 g4589566 1.00E−45 KIAA0961 protein 469 3 246 228 965 g487787 2.00E−37 zinc finger protein ZNF140 470 1 107 40 360 g14348591 2.00E−28 KRAB zinc finger protein 470 1 107 40 360 g7959207 1.00E−27 KIAA1473 protein 470 1 107 40 360 g186774 4.00E−27 zinc finger protein 471 3 357 3 1073 g12052983 1.00E−167 hypothetical protein 471 3 357 3 1073 g14042293 1.00E−135 unnamed protein product 471 3 357 3 1073 g5262560 1.00E−113 hypothetical protein 472 3 90 3 272 g13752754 2.00E−16 zinc flnger 1111 472 3 90 3 272 g14348588 9.00E−15 KRAB zinc finger protein 472 3 90 3 272 g12654015 9.00E−15 Similar to hypothetical protein FLJ10891 473 1 295 1 885 g14495650 1.00E−75 (BC009433) zinc finger protein 331; zinc finger protein 463 473 1 295 1 885 g8575775 1.00E−75 KRAB zinc finger protein 473 1 295 1 885 g13939858 1.00E−75 RITA 474 1 195 1 585 g7020503 9.00E−68 unnamed protein product 474 1 195 1 585 g8453103 1.00E−67 zinc finger protein 474 1 195 1 585 g8099348 3.00E−67 zinc finger protein 475 2 232 257 952 g14042293 4.00E−53 unnamed protein product 475 2 232 257 952 g14042850 3.00E−47 unnamed protein product 475 2 232 257 952 g12052983 6.00E−38 hypothetical protein 476 2 282 2 847 g10440398 1.00E−93 FLJ00032 protein 476 2 282 2 847 g10047297 1.00E−93 KIAA1611 protein 476 2 282 2 847 g10436789 8.00E−93 unnamed protein product 477 3 149 3 449 g12656631 7.00E−20 Kruppel-like zinc finger protein GLIS2 477 3 149 3 449 g13507039 2.00E−19 Gli-Kruppel zinc-finger protein NKL 477 3 149 3 449 g13507037 2.00E−19 Gli-Kruppel zinc-finger protein NKL 478 3 283 3 851 g13623633 1.00E−174 Unknown (protein for MGC: 13105) 478 3 283 3 851 g488555 3.00E−98 zinc finger protein ZNF135 478 3 283 3 851 g10437767 9.00E−97 unnamed protein product 479 3 264 3 794 g6807587 1.00E−124 hypothetical protein 479 3 264 3 794 g5931821 1.00E−124 dJ228H13.3 (zinc finger protein) 479 3 264 3 794 g488555 1.00E−96 zinc finger protein ZNF135 480 1 201 430 1032 g3540177 1.00E−117 F23269_2 480 1 201 430 1032 g5080758 6.00E−92 BC331191_1 480 1 201 430 1032 g12855931 1.00E−55 putative 481 1 283 880 1728 g14017871 1.00E−143 KIAA1827 protein 481 1 283 880 1728 g10436789 2.00E−97 unnamed protein product 481 1 283 880 1728 g13752754 1.00E−95 zinc finger 1111 482 2 101 131 433 g14042373 1.00E−24 unnamed protein product 482 2 101 131 433 g1389741 7.00E−24 KRAB/zinc finger suppressor protein 1 482 2 101 131 433 g9800824 2.00E−20 bA179N14.1 (novel zinc finger protein) 483 1 101 112 414 g13937999 3.00E−48 Similar to DNA-binding protein 483 1 101 112 414 g3329372 1.00E−34 DNA-binding protein 483 1 101 112 414 g12052732 3.00E−34 hypothetical protein 484 2 297 215 1105 g12862320 2.00E−51 WDC146 486 3 108 462 785 g12856025 1.00E−51 putative 486 3 108 462 785 g12846941 4.00E−37 putative 486 3 108 462 785 g13938537 2.00E−36 Similar to RIKEN cDNA 4933430F16 gene 487 2 122 122 487 g4235144 4.00E−47 BC39498_1 487 2 122 122 487 g4235143 7.00E−34 BC39498_3 487 2 122 122 487 g8163824 4.00E−30 krueppel-like zinc finger protein HZF2 488 1 182 148 693 g12854977 1.00E−41 putative 488 1 182 148 693 g7267246 1.00E−21 putative adenosine deaminase 488 1 182 148 693 g7299138 1.00E−16 CG11994 gene product 489 2 114 293 634 g5262523 3.00E−19 hypothetical protein 489 2 114 293 634 g340170 3.00E−19 orotidine 5′-monophosphate decarboxylase (EC4.1.1.23) 489 2 114 293 634 g340168 3.00E−19 UMP synthase 490 3 415 3 1247 g2689442 0 R28830_1 490 3 415 3 1247 g1572600 1.00E−172 Zik1 490 3 415 3 1247 g12652759 1.00E−141 hypothetical protein FLJ20557 491 3 43 348 476 g12052884 3.00E−06 hypothetical protein 491 3 43 348 476 g7023332 4.00E−06 unnamed protein product 491 3 43 348 476 g183002 6.00E−05 guanylate binding protein isoform I 492 1 134 49 450 g220637 4.00E−52 zinc finger protein 492 1 134 49 450 g5730196 2.00E−51 Kruppel-type zinc finger 492 1 134 49 450 g14456631 8.00E−51 dJ54B20.4 (novel KRAB box containing C2H2 type zinc finger protein) 493 3 239 3 719 g14042330 2.00E−96 unnamed protein product 493 3 239 3 719 g10954044 8.00E−92 KRAB zinc finger protein ZFQR 493 3 239 3 719 g10442700 8.00E−92 zinc-finger protein ZBRK1 495 2 185 134 688 g13560888 2.00E−38 EZFIT-related protein 1 495 2 185 134 688 g7243243 2.00E−37 KIAA1431 protein 495 2 185 134 688 g4567178 5.00E−35 R31665_2 (AA 1-673) 496 1 277 178 1008 g4589588 4.00E−67 KIAA0972 protein 496 1 277 178 1008 g498152 4.00E−51 ha0946 protein is Kruppel-related. 496 1 277 178 1008 g6467204 3.00E−38 gonadotropin inducible transcription repressor-3 497 3 241 3 725 g14043841 3.00E−41 Unknown (protein for MGC: 14429) 497 3 241 3 725 g14042293 6.00E−41 unnamed protein product 497 3 241 3 725 g12052983 2.00E−40 hypothetical protein 498 2 251 1139 1891 g12052983 1.00E−114 hypothetical protein 498 2 251 1139 1891 g5262560 4.00E−68 hypothetical protein 498 2 251 1139 1891 g10434856 1.00E−61 unnamed protein product 499 3 282 54 899 g5080758 1.00E−103 BC331191_1 499 3 282 54 899 g3540177 1.00E−103 F23269_2 499 3 282 54 899 g12855931 1.00E−58 putative 500 1 442 28 1353 g12652727 0 Unknown (protein for IMAGE: 3352566) 500 1 442 28 1353 g488555 1.00E−97 zinc finger protein ZNF135 500 1 442 28 1353 g3378094 1.00E−95 KRAB domain zinc finger protein 501 3 292 3 878 g488551 1.00E−97 zinc finger protein ZNF132 501 3 292 3 878 g13543419 2.00E−97 Similar to zinc finger protein 304 501 3 292 3 878 g1199604 3.00E−97 zinc finger protein C2H2-25 502 1 166 1 498 g12804419 2.00E−65 Unknown (protein for MGC: 1136) 502 1 166 1 498 g12844790 5.00E−64 putative 502 1 166 1 498 g13111895 3.00E−33 Unknown (protein for MGC: 2627) 504 1 406 1 1218 g12053281 0 hypothetical protein 504 1 406 1 1218 g12836135 1.00E−167 putative 504 1 406 1 1218 g3043598 2.00E−64 KIAA0537 protein 505 1 332 1 996 g10438696 1.00E−140 unnamed protein product 505 1 332 1 996 g12847740 7.00E−11 putative 505 1 332 1 996 g7022551 1.00E−09 unnamed protein product 506 2 183 2 550 g4105619 1.00E−94 SPAF 506 2 183 2 550 g12847023 1.00E−94 putative 506 2 183 2 550 g7297973 5.00E−67 CG5776 gene product

[0307] TABLE 8 Parameter Program Description Reference Threshold ABIFACTURA A program that removes vector sequences and Applied Biosystems, Foster City, CA. masks ambiguous bases in nucleic acid sequences. ABI/ A Fast Data Finder useful in comparing and Applied Biosystems, Foster City, CA; Mismatch PARACEL annotating amino acid or nucleic acid sequences. Paracel Inc., Pasadena, CA. <50% FDF ABI A program that assembles nucleic acid sequences. Applied Biosystems, Foster City, CA. AutoAssembler BLAST A Basic Local Alignment Search Tool useful in Altschul, S. F. et al. (1990) J. Mol. Biol. ESTs: sequence similarity search for amino acid and 215: 403-410; Altschul, S. F. et al. (1997) Probability nucleic acid sequences. BLAST includes five Nucleic Acids Res. 25: 3389-3402. value = 1.0E−8 functions: blastp, blastn, blastx, tblastn, and tblastx. or less Full Length sequences: Probability value = 1.0E−10 or less FASTA A Pearson and Lipman algorithm that searches for Pearson, W. R. and D. J. Lipman (1988) Proc. ESTs: fasta E similarity between a query sequence and a group of Natl. Acad Sci. USA 85: 2444-2448; Pearson, value = sequences of the same type. FASTA comprises as W. R. (1990) Methods Enzymol. 183: 63-98; 1.06E−6 least five functions: fasta, tfasta, fastx, tfastx, and and Smith, T. F. and M. S. Waterman (1981) Assembled ssearch. Adv. Appl. Math. 2: 482-489. ESTs: fasta Identity = 95% or greater and Match length = 200 bases or greater; fastx E value = 1.0E−8 or less Full Length sequences: fastx score = 100 or greater BLIMPS A BLocks IMProved Searcher that matches a Henikoff, S. and J. G. Henikoff (1991) Nucleic Probability sequence against those in BLOCKS, PRINTS, Acids Res. 19: 6565-6572; Henikoff, J. G. and value = 1.0E−3 DOMO, PRODOM, and PFAM databases to search S. Henikoff (1996) Methods Enzymol. or less for gene families, sequence homology, and structural 266: 88-105; and Attwood, T. K. et al. (1997) J. fingerprint regions. Chem. Inf. Comput. Sci. 37: 417-424. HMMER An algorithm for searching a query sequence against Krogh, A. et al. (1994) J. Mol. Biol. PEAM hits: hidden Markov model (HMM)-based databases of 235: 1501-1531; Sonnhammer, E. L. L. et al. Probability protein family consensus sequences, such as PFAM. (1988) Nucleic Acids Res. 26: 320-322; value = 1.0E−3 Durbin, R. et al. (1998) Our World View, in a or less Nutshell, Cambridge Univ. Press, pp. 1-350. Signal peptide hits: Score = 0 or greater ProfileScan An algorithm that searches for structural and sequence Gribskov, M. et al. (1988) CABIOS 4: 61-66; Normalized motifs in protein sequences that match sequence patterns Gribskov, M. et al. (1989) Methods Enzymol. quality score ≧ defined in Prosite. 183: 146-159; Bairoch, A. et al. (1997) GCG-specified Nucleic Acids Res. 25: 217-221. “HIGH” value for that particular Prosite motif. Generally, score = 1.4-2.1. Phred A base-calling algorithm that examines automated Ewing, B. et al. (1998) Genome Res. sequencer traces with high sensitivity and probability. 8: 175-185; Ewing, B. and P. Green (1998) Genome Res. 8: 186-194. Phrap A Phils Revised Assembly Program including SWAT and Smith, T. F. and M. S. Waterman (1981) Adv. Score = 120 or CrossMatch, programs based on efficient implementation Appl. Math. 2: 482-489; Smith, T.F. and M.S. greater; of the Smith-Waterman algorithm, useful in searching Waterman (1981) J. Mol. Biol. 147: 195-197; Match length = sequence homology and assembling DNA sequences. and Green, P., University of Washington, 56 or greater Seattle, WA. Consed A graphical tool for viewing and editing Phrap assemblies. Gordon, D. et al. (1998) Genome Res. 8: 195-202. SPScan A weight matrix analysis program that scans protein Nielson, H. et al. (1997) Protein Engineering Score = 3.5 or sequences for the presence of secretory signal peptides. 10: 1-6; Claverie, J.M. and S. Audic (1997) greater CABIOS 12: 431-439. TMAP A program that uses weight matrices to delineate Persson, B. and P. Argos (1994) J. Mol. Biol. transmembrane segments on protein sequences and 237: 182-192; Persson, B. and P. Argos (1996) determine orientation. Protein Sci. 5: 363-371. TMHMMER A program that uses a hidden Markov model (HMM) to Sonnhammer, E. L. et al. (1998) Proc. Sixth Intl. delineate transmembrane segments on protein sequences Conf. on Intelligent Systems for Mol. Biol., and determine orientation. Glasgow et al., eds., The Am. Assoc. for Artificial Intelligence(AAAI) Press, Menlo Park, CA, and MIT Press, Cambridge, MA, pp. 175-182. Motifs A program that searches amino acid sequences for patterns Bairoch, A. et al. (1997) Nucleic Acids that matched those defined in Prosite. Res. 25: 217-221; Wisconsin Package Program Manual, version 9, page M51-59, Genetics Computer Group, Madison, WI. 

What is claimed is:
 1. An isolated polynucleotide selected from the group consisting of: a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252, b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:1-252, c) a polynucleotide complementary to the polynucleotide of a), d) a polynucleotide complementary to the polynucleotide of b), and e) an RNA equivalent of a)-d).
 2. An isolated polynucleotide of claim 1, selected from the group consisting of SEQ ID NO:1-252.
 3. An isolated polynucleotide comprising at least 30 contiguous nucleotides of a polynucleotide of claim
 1. 4. An isolated polynucleotide comprising at least 60 contiguous nucleotides of a polynucleotide of claim
 1. 5. A composition for the detection of expression of disease detection and treatment polynucleotides comprising at least one of the polynucleotides of claim 1 and a detectable label.
 6. A method for detecting a target polynucleotide in a sample, said target polynucleotide having a sequence of a polynucleotide of claim 1, the method comprising: a) amplifying said target polynucleotide or fragment thereof using polymerase chain reaction amplification, and b) detecting the presence or absence of said amplified target polynucleotide or fragment thereof, and, optionally, if present, the amount thereof.
 7. A method for detecting a target polynucleotide in a sample, said target polynucleotide having a sequence of a polynucleotide of claim 1, the method comprising: a) hybridize

sample with a probe comprising at least

contiguous nucleotides comprising a sequence complementary to said target polynucleotide in the sample, and which probe specifically hybridizes to said target polynucleotide, under conditions whereby a hybridization complex is formed between said probe and said target polynucleotide or fragments thereof, and b) detecting the presence or absence of said hybridization complex, and, optionally, if present, the amount thereof.
 8. A method of claim 7, wherein the probe comprises at least 30 contiguous nucleotides.
 9. A method of claim 7, wherein the probe comprises at least 60 contiguous nucleotides.
 10. A recombinant polynucleotide comprising a promoter sequence operably linked to a polynucleotide of claim
 1. 11. A cell transformed with a recombinant polynucleotide of claim
 10. 12. A transgenic organism comprising a recombinant polynucleotide of claim
 10. 13. A method for producing a disease detection and treatment polypeptide encoded by a polynucleotide of claim 1, the method comprising: a) culturing a cell under conditions suitable for expression of the disease detection and treatment polypeptide, wherein said cell is transformed with a recombinant polynucleotide comprising a promoter sequence operably linked to a polynucleotide of claim 1, and b) recovering the disease detection and treatment polypeptide so expressed.
 14. A method of claim 13, wherein the polypeptide has an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.
 15. An isolated disease detection and treatment polypeptide (MDDT) encoded by at least one of the polynucleotides of claim
 2. 16. A method of screening for a test compound that specifically binds to the polypeptide of claim 15, the method comprising: a) combining the polypeptide of claim 15 with at least one

compound under suitable conditions, and b) detecting binding of the polypeptide of claim 15 to the test compound, thereby identifying a compound that specifically binds to the polypeptide of claim
 15. 17. A microarray wherein at least one element of the microarray is a polynucleotide of claim
 3. 18. A method for generating a transcript image of a sample which contains polynucleotides, the method comprising: a) labeling the polynucleotides of the sample, b contacting the elements of the microarray of claim 17 with the labeled polynucleotides of the sample under conditions suitable for the formation of a hybridization complex, and c) quantifying the expression of the polynucleotides in the sample.
 19. A method for screening a compound for effectiveness in altering expression of a target polynucleotide, wherein said target polynucleotide comprises a polynucleotide sequence of a polynucleotide of claim 1, the method comprising: a) exposing a sample comprising the target polynucleotide to a compound, under conditions suitable for the expression of the target polynucleotide, b) detecting altered expression of the target polynucleotide, and c) comparing the expression of the target polynucleotide in the presence of varying amounts of the compound and in the absence of the compound.
 20. A method for assessing toxicity of a test compound, said method comprising: a) treating a biological sample containing nucleic acids with the test compound, b) hybridizing the nucleic acids of the treated biological sample with a probe comprising at least 20 contiguous nucleotides of a polynucleotide of claim 1 under conditions whereby a specific hybridization complex is formed between said probe and a target polynucleotide in the biological sample, said target polynucleotide comprising a polynucleotide sequence of a polynucleotide of claim 1 or fragment thereof, c) quantifying the amount of hybridization complex, and d) comparing the amount of hybridization complex in the treated biological sample with the amount of hybridization complex in an untreated biological sample, wherein a difference in the amount of hybridization complex in the untreated biological sample is indicative of toxicity of the test compound.
 21. An array comprising different nucleotide molecules affixed in distinct physical locations on a solid substrate, wherein at least one of said nucleotide molecules comprises a first oligonucleotide or polynucleotide sequence specifically hybridizable with at least 30 contiguous nucleotides of a target polynucleotide, and wherein said target polynucleotide is a polynucleotide of claim
 1. 22. An array of claim 21, wherein said first oligonucleotide or polynucleotide sequence is completely complementary to at least 30 contiguous nucleotides of said target polynucleotide.
 23. An array of claim 21, wherein said first oligonucleotide or polynucleotide sequence is completely complementary to at least 60 contiguous nucleotides of said target polynucleotide
 24. An array of claim 21, wherein said first oligonucleotide or polynucleotide sequence is completely complementary to said target polynucleotide.
 25. An array of claim 21, which is a microarray.
 26. An array of claim 21, further comprising said target polynucleotide hybridized to a nucleotide molecule comprising said first oligonucleotide or polynucleotide sequence.
 27. An array of claim 21, wherein a linker joins at least one of said nucleotide molecules to said solid substrate.
 28. An array of claim 21, wherein each distinct physical location on the substrate contains multiple nucleotide molecules, and the multiple nucleotide molecules at any single distinct physical location have the same sequence, and each distinct physical location on the substrate contains nucleotide molecules having a sequence which differs from the sequence of nucleotide molecules at another distinct physical location on the substrate.
 29. An isolated polypeptide selected from the group consisting of: a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical

amino acid sequence selected from the g

consisting of SEQ ID NO:253-506, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.
 30. An isolated polypeptide of claim 29, having a sequence selected from the group consisting of SEQ ID NO:253-506.
 31. An isolated polynucleotide encoding a polypeptide of claim
 29. 32. An isolated polynucleotide encoding a polypeptide of claim
 30. 33. An isolated polynucleotide of claim 32, having a sequence selected from the group consisting of SEQ ID NO:1-252.
 34. An isolated antibody which specifically binds to a disease detection and treatment polypeptide of claim
 29. 35. A diagnostic test for a condition or disease associated with the expression of MDDT in a biological sample, the method comprising: a) combining the biological sample with an antibody of claim 34, under conditions suitable for the antibody to bind the polypeptide and form an antibody:polypeptide complex, and b) detecting the complex, wherein the presence of the complex correlates with the presence of the polypeptide in the biological sample.
 36. The antibody of claim 34, wherein the antibody is: a) a chimeric antibody, b) a single chain antibody, c) a Fab fragment, d) a F(ab′)₂ fragment, or e) a humanized antibody.
 37. A composition comprising an antibody of claim 34 and an

ptable excipient.
 38. A method of diagnosing a condition or disease associated with the expression of MDDT in a subject, comprising administering to said subject an effective amount of the composition of claim
 37. 39. A composition of claim 37, wherein the antibody is labeled.
 40. A method of diagnosing a condition or disease associated with the expression of MDDT in a subject, comprising administering to said subject an effective amount of the composition of claim
 39. 41. A method of preparing a polyclonal antibody with the specificity of the antibody of claim 34, the method comprising: a) immunizing an animal with a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, or an immunogenic fragment thereof, under conditions to elicit an antibody response, b) isolating antibodies from said animal, and c) screening the isolated antibodies with the polypeptide, thereby identifying a polyclonal antibody which binds specifically to a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.
 42. An antibody produced by a method of claim
 41. 43. A composition comprising the antibody of claim 42 and a suitable carrier.
 44. A method of making a monoclonal antibody with the specificity of the antibody of claim 34, the method comprising: a) immunizing an animal with a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506, or an immunogenic fragment thereof, under conditions to elicit an antibody response, b) isolating antibody producing cells from the animal, c) fusing the antibody producing cells with immortalized cells to form monoclonal antibody-producing hybridoma cells, d) culturing

hybridoma cells, and e) isolating from the culture monoclonal antibody which binds specifically to a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.
 45. A monoclonal antibody produced by a method of claim
 44. 46. A composition comprising the antibody of claim 45 and a suitable carrier.
 47. The antibody of claim 34, wherein the antibody is produced by screening a Fab expression library.
 48. The antibody of claim 34, wherein the antibody is produced by screening a recombinant immunoglobulin library.
 49. A method of detecting a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506 in a sample, the method comprising: a) incubating the antibody of claim 34 with a sample under conditions to allow specific binding of the antibody and the polypeptide, and b) detecting specific binding, wherein specific binding indicates the presence of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506 in the sample.
 50. A method of purifying a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506 from a sample, the method comprising: a) incubating the antibody of claim 34 with a sample under conditions to allow specific binding of the antibody and the polypeptide, and b) separating the antibody from the sample and obtaining the purified polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:253-506.
 51. A composition comprising a polypeptide of claim 29 and a pharmaceutically acceptable excipient.
 52. A composition of claim 51, wherein the polypeptide has an amino acid sequence of SEQ ID NO:253-506.
 53. A method for treating a disease or condition associated with increased expression of functional MDDT, comprising administering to a patient in need of such treatment the composition of claim
 51. 54. A method for screening a compound for effectiveness as an agonist of a polypeptide of claim 29, the method comprising: a) exposing a sample comprising a polypeptide of claim 29 to a compound, and b) detecting agonist activity in the sample.
 55. A composition comprising an agonist compound identified by a method of claim 54 and a pharmaceutically acceptable excipient.
 56. A method for treating a disease or condition associated with decreased expression of functional MDDT, comprising administering to a patient in need of such treatment a composition of claim
 55. 57. A method for screening a compound for effectiveness as an antagonist of a polypeptide of claim 29, the method comprising: a) exposing a sample comprising a polypeptide of claim 29 to a compound, and b) detecting antagonist activity in the sample.
 58. A composition comprising an antagonist compound identified by a method of claim 57 and a pharmaceutically acceptable excipient.
 59. A method for treating a disease or condition associated with overexpression of functional MDDT, comprising administering to a patient in need of such treatment a composition of claim
 58. 60. A method of screening for a compound that modulates the activity of the polypeptide of claim 29, said method comprising: a) combining the polypeptide of claim 29 with at least one test compound under conditions permissive for the activity of the polypeptide of claim 29, b) assessing the activity of the polypeptide of claim 29 in the presence of the test compound, and c) comparing the activity of the polypeptide of claim 29 in the presence of the test compound with the activity of the polypeptide of claim 29 in the absence of the test compound wherein a change in the activity of the polypeptide of claim 29 in the presence of the test compound is indicative of a compound that modulates the activity of the polypeptide of claim
 29. 